Mariusz Jaskolski

Selected publications, listed by subject or back to homepage

Retroviral proteases

• M.Miller, M.Jaskolski, J.K.Mohana Rao, J.Leis, A.Wlodawer:
  Crystal structure of a retroviral protease proves relationship to aspartic protease family.
  Nature 337, 576-579 (1989). [PubMed]
• I.T.Weber, M.Miller, M.Jaskolski, J.Leis, A.M.Skalka, A.Wlodawer:
  Molecular Modeling of the HIV-1 Protease and Its Substrate Binding Site.
  Science 243, 928-931 (1989). [PubMed]
• A.Wlodawer, M.Miller, M.Jaskolski,B.K.Sathyanarayana, E.Baldwin, I.T.Weber, L.M.Selk, L.Clawson, J.Schneider, S.B.H.Kent:
  Conserved Folding in Retroviral Proteases: Crystal Structure of a Synthetic HIV-1 Protease.
  Science 245, 616-621 (1989). [PubMed]
• M.Jaskolski, M.Miller, J.K.M.Rao, J.Leis, A.Wlodawer (1989),
  Structure of the aspartic protease from Raus sarcoma retrovirus at 2 A resolution.
  In: Viral Proteinases as Targets for Chemotherapy, H.-G.Krausslich, S.Oroszlan, E.Wimmer, eds. Cold Spring Harbor Laboratory: Cold Spring Harbor, NY, pp. 175-180.
• S.I.Foundling, F.R.Salemme, B.Korant, J.J.Wendolowski, P.C.Weber, A.C.Treharne, M.C.Schadt, M.Jaskolski, M.Miller, A.Wlodawer, P.Strop, V.Kostka, J.Sedlacek, D.H.Ohlendorf (1989),
  Crystal structure of a retroviral protease from avian myeloblastosis associated virus.
  In: Viral Proteinases as Targets for Chemotherapy, H.-G.Krausslich, S.Oroszlan, E.Wimmer, eds. Cold Spring Harbor Laboratory: Cold Spring Harbor, NY, pp. 181-190.
• M.Jaskolski, M.Miller, J.K.M.Rao, J.Leis, A.Wlodawer:
  Structure of the Aspartic Protease from Rous sarcoma Retrovirus Refined at 2-A Resolution.
  Biochemistry 29, 5889-5898 (1990). [PubMed]
• M.Miller, A.L.Swain, M.Jaskolski, B.K.Sathyanarayana, G.R.Marshall, D.Rich, S.B.H.Kent, A.Wlodawer (1990),
  X-ray Analysis of HIV-1 Protease and Its Complexes with Inhibitors.
  In: Retroviral Proteases: Control of Maturation and Morphogenesis, L.Pearl, ed. MacMillan Press, pp. 93-106.
• M.Jaskolski, A.G.Tomasselli, T.K.Sawyer, D.G.Staples, R.L.Heinrikson, J.Schneider, S.B.H.Kent, A.Wlodawer:
  Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
  Biochemistry 30, 1600-1609 (1991). [PubMed]
• T.Sawyer, D.Staples, L.Liu, A.Tomaselli, B.Dunn, W.Lowther, J.Hinzmann, R.Poorman, A.Wlodawer, M.Jaskolski:
  HIV Protease (HIV PR) Inhibitor Structure-Activity, Selectivity and Active Site Molecular Modeling of High Affinity Leu-psi-[CH(OH)CH2]Val Modified Viral and Nonviral Substrate Analogs.
  Int. J. Peptide Protein Res.40, 274-281 (1992). [PubMed]
• E.Buchtelova, J.Hasek, J.Dohnalek, E.Tykarska, M.Jaskolski, L.Olivi:
  Preliminary crystallographic study of native HIV-1 protease inhibited by hydroxyethylamine modified tetraopeptides of Boc-Phe-psi[(R/S)-CH(OH)CH2NH]Phe-Ile-Phe-NH2 type.
  Materials Structure 6, 6-7 (1999).
• E.Buchtelova, J.Hasek, J.Dohnalek, H.Petrokova, J.Duskova, T.Skalova, J.Brynda, J.Sedlacek, M.Hradilek, J.Konvalinka, E.Tykarska, M.Jaskolski, L.Olivi:
  Product of autodigestion at Leu63-Ile64 site binds to HIV-1 protease instead of inhibitor Boc-Phe-psi[(S)-CH(OH)CH2NH]Phe-Ile-Phe-NH2.
  Materials Structure 8, 31-32 (2001).
• A.Hilgeroth, E.Tykarska, M.Jaskolski (2002),
  Crystal structure of a novel synthetic inhibitor of HIV-1 protease.
  J. Mol. Struct. 605, 63-70.
• M.Li, G.Laco, M.Jaskolski, J.Rozycki, J.Alexandratos, A.Wlodawer, A.Gustchina (2005),
  Crystal structure of HTLV protease: From treating AIDS to fighting cancer.
  Proc. Natl. Acad. Sci. USA. 102, 18332-18337. [PubMed]
• M.Jaskolski, A.Gustchina, A.Wlodawer (2006),
  Lessons learned fighting HIV can be applied to anti-cancer drug design.
  Cell Cycle 5, 463-464. [PubMed]
• M.Jaskolski (2009),
  Proteazy retrowirusowe po 20 latach: reminiscencje.
  Postepy Biochemii, 55, 15-20. [PubMed]
• F.Khatib, F.DiMaio, Foldit Contenders Group, Foldit Void Crushers Group, S.Cooper, M.Kazmierczyk, M.Gilski, Sz.Krzywda, H.Zabranska, I.Pichova, J.Thompson, Z.Popovic, M.Jaskolski, D.Baker (2011),
  Crystal structure of monomeric retroviral protease solved by protein folding game players.
  Nature Struct. Mol. Biol. 18, 1175-1177. doi:10.1038/nsmb.2119. [PubMed]
• M.Gilski, M.Kazmierczyk, Sz.Krzywda, H.Zabranska, S.Cooper, Z.Popovic, F.Khatib, F.DiMaio, J.Thompson, D.Baker, I.Pichova, M.Jaskolski (2011),
  High-resolution structure of retroviral protease folded as a monomer.
  Acta Cryst. D67, 907-914. [PubMed]
• M.Jaskolski, M.Miller, J.K.M.Rao, A.Gustchina, A.Wlodawer (2015),
  Elucidation of the structure of retroviral proteases: a reminiscence.
  FEBS J. 282, 4059-4066. [PDF]
• A.Wlodawer, M.Jaskolski (2016),
  Inhibitors of HIV protease.
  In: Encyclopedia of Cell Biology, R.A.Bradshaw, P.Stahl, eds., pp. 738-745, Elsevier.
• S.Wosicki, M.Gilski, H.Zabranska, I.Pichova, M.Jaskolski (2019),
  Comparison of a retroviral protease in monomeric and dimeric states.
  Acta Cryst. D75, 904-917. [PDF]
• S.Wosicki, M.Kazmierczyk, M.Gilski, H.Zabranska, I.Pichova, M.Jaskolski (2021),
  Crystal structures of inhibitor complexes of M-PMV protease with visible flap loops. Protein Sci. 30, 1258-1263. [OpenAccess]
• A.Wlodawer, M.Jaskolski (2022) Inhibitors of HIV Protease and Their Role as Drugs Against AIDS. In: Reference Module in Life Sciences, Roitberg Bernard D. (eds.), 1-10, Elsevier Reference Collection, Elsevier, ISBN 978-0-12-809633-8. DOI: 10.1016/B978-0-12-821618-7.00024-9 [DOI]

Retroviral integrase

• G.Bujacz, M.Jaskolski, J.Alexandratos, A.Wlodawer, G.Merkel, R.A.Katz, A.M.Skalka:
  The Catalytic Domain of Avian Sarcoma Virus Integrase: Conformation of the Active-site Residues in the Presence of Divalent Cations.
  Structure 4, 89-96 (1996). [PubMed]
• G.Bujacz, M.Jaskolski, J.Alexandratos, A.Wlodawer, G.Merkel, R.A.Katz, A.M.Skalka:
  High-resolution structure of the catalytic domain of Avian sarcoma virus integrase.
  J. Mol. Biol. 253, 333-346 (1995). [PubMed]
• G.Bujacz, M.Jaskolski, J.Alexandratos, A.Wlodawer, G.Merkel, R.A.Katz, A.M.Skalka:
  Crystal structure of the catalytic domain of avian sarcoma virus integrase.
  In: Techniques in Protein Chemistry VII, ed. D.R.Marshak, pp. 383-389, Academic Press, 1996.
• J.Alexandratos, G.Bujacz, M.Jaskolski, A.Wlodawer, G.Merkel, R.A.Katz, A.M.Skalka:
  Crystal structure of avian sarcoma virus integrase with bound essential cations.
  In: Techniques in Protein Chemistry VIII, ed. D.R.Marshak, pp. 417-425, Academic Press, 1997.
• M.Jaskolski, J.Alexandratos, G.Bujacz, A.Wlodawer (2009),
  Piecing together the structure of retroviral integrase, an important target in AIDS therapy.
  FEBS J. 276, 2936-2946. [PubMed]
• M.Jaskolski, J.N.Alexandratos, G.Bujacz, A.Wlodawer (2011),
  Structural studies of retroviral integrases. In: Retroviral Integrase (ed. N.Neamati). pp. 35-49. Wiley.

L-Asparaginases

• A.L.Swain, M.Jaskolski, D.Housset, J.K.M.Rao, A.Wlodawer:
  Crystal structure of E. coli L-asparaginase, an enzyme used in cancer therapy.
  Proc. Natl. Acad. Sci. USA 90, 1474-1478 (1993). [PubMed]
• D.Bonthron, M.Jaskolski:
  Why a "benign" mutation kills enzyme activity. Structure-based analysis of the A176V mutant of S. cerevisiae L-asparaginase I.
  Acta Biochim. Polon. 44, 491-504 (1997). [PubMed]
• M.Jaskolski:
  L-Asparaginase - an Anticancer Drug and Challenge for Crystallography.
  Modern Cancer Treat. 1, 10-11 (1998).
• D.Borek, J.Podkowinski, A.Kisiel, M.Jaskolski:
  Isolation and characterization of cDNA encoding L-asparaginase from Lupinus luteus (PGR99-050).
  Plant Physiol. 119, 1568-1569 (1999).
• M.Kozak, M.Jaskolski:
  Crystallization and preliminary crystallographic studies of a new crystal form of Escherichia coli L-asparaginase II (Ser58Ala mutant).
  Acta Cryst. D56, 509-511 (2000). [PubMed]
• D.Borek, M.Jaskolski:
  Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome.
  Acta Cryst. D56, 1505-1507 (2000). [PubMed]
• M.Kozak, M.Jaskolski, K.H.Rohm:
  Preliminary crystallographic studies of Y25F mutant of periplasmic Escherichia coli asparaginase.
  Acta Biochim. Polon. 47, 807-814 (2000). [PDF]
• M.Jaskolski, M.Kozak, J.Lubkowski, G.Palm, A.Wlodawer:
  Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
  Acta Cryst. D57, 369-377 (2001). [PubMed]
• M.Kozak, D.Borek, M.Janowski, M.Jaskolski:
  Crystallization of D90E mutant of Escherichia coli L-asparaginase II in five crystal forms.
  Acta Cryst. D58, 130-132 (2002). [PubMed]
• D.Borek, M.Jaskolski:
  Sequence analysis of enzymes with asparaginase activity.
  Acta Biochim. Polon. 48, 893-902 (2001). [PDF]
• D.Borek, K.Michalska, K.Brzezinski, A.Kisiel, J.Podkowinski, D.T.Bonthron, D.Krowarsch, J.Otlewski, M.Jaskolski (2004),
  Expression, purification, and catalytic activity of Lupinus luteus asparagine b-amidohydrolase and its Escherichia coli homolog.
  Eur. J. Biochem.271, 3215-3226. [PubMed]
• K.Michalska, K.Brzezinski, M.Jaskolski (2005),
  Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate.
  J. Biol. Chem. 280, 28484-28491. [PubMed]
• K.Michalska, G.Bujacz, M.Jaskolski (2006),
  Crystal structure of plant asparaginase.
  J. Mol. Biol. 360, 105-116. [PubMed]
• K.Michalska, M.Jaskolski (2006),
  Structural aspects of L-asparaginases, their friends and relations.
  Acta Biochim. Polon. 53, 627-640. [PDF]
• K.Michalska, D.Borek, A.Hernandez-Santoyo, M.Jaskolski (2008),
  Crystal packing of plant-type L-asparaginase from Escherichia coli.
  Acta Cryst. D64, 309-320. [PubMed]
• K.Michalska, A.Hernandez-Santoyo, M.Jaskolski (2008),
  The mechanism of autocatalytic activation of plant-type L-asparaginases.
  J. Biol. Chem. 283, 13388-13397. [PubMed]
• K.Michalska, M.Jaskolski (2012),
  Isoaspartyl aminopeptidase (threonine type). In The Handbook of Proteolytic Enzymes, N.D.Rawlings & G.Salvesen, eds. Elsevier.
  
• M.Bejger, B.Imiolczyk, D.Clavel, M.Gilski, A.Pajak, F.Marsolais, M.Jaskolski (2014),
  Na+/K+ exchange switches the catalytic apparatus of K-dependent plant L-asparaginase.
  Acta Cryst. D70, 1854-1872. [PubMed]
• D.Borek, M.Kozak, J.Pei, M.Jaskolski (2014),
  Crystal structure of active-site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site.
  FEBS J. 281, 4097-4111. [PubMed]
• E.Ajewole, L.Santamaria-Kisiel, A.Pajak, M.Jaskolski, F.Marsolais (2018),
  Structural basis of the potassium activation in plant asparaginases.
  FEBS J. 285, 1528-1539. [PubMed]
• J.Loch, M.Jaskolski (2021),
  Structural and biophysical aspects of L-asparaginases - a growing family with amazing diversity.
  IUCrJ 8, 514-531. [OpenAccess]
• J.I.Loch, B.Imiolczyk, J.Sliwiak, A.Wantuch, M.Bejger, M.Gilski, M.Jaskolski (2021),
  Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.
  Nature Commun. 12, 6717. [OpenAccess] https://rdcu.be/cByos
• J.I.Loch, A.Klonecka, K.Kadziolka, P.Bonarek, J.Barciszewski, B.Imiolczyk, K.Brzezinski, M.Jaskolski (2022),
  Structural and biophysical studies of new L-asparaginase variants: lessons from random mutagenesis of the prototypic E. coli Ntn-hydroalse.
  Acta Cryst. D78, 911-926. DOI: 10.1107/S2059798322005691 [OpenAccess]
• A.Zielezinski, J.Loch, W.M.Karlowski, M.Jaskolski (2022),
  Massive annotation of bacterial L-asparaginases reveals their puzzling distribution and frequent gene transfer events.
  Sci. Rep. 12:15797. DOI: 10.1038/s41598-022-19689-1 [OpenAccess]
• M.Janicki, A.Sciuk, J.I.Loch, A.Zielezinski, M.Ruszkowski, A.Ludwikow, W.M.Karlowski, M.Jaskolski (2023),
  The effects of nature-inspired amino acid substitutions on structural and biochemical properties of the E. coli L-asparaginase EcAIII.
  Protein Sci. 32, e-4647. DOI: 10.1002/pro.4647 [OpenAccess]
• J.L.Loch, P.Worsztynowicz, J.Sliwiak, M.Grzechowiak, B.Imiolczyk, K.Pokrywka, M.Chwastyk, M.Gilski, M.Jaskolski (2023),
  Rhizobium etli has two L-asparaginases of low sequence identity but similar structure and catalytic center.
  Acta Cryst. D79, 775-791. DOI: 10.1107/S2059798323005648
• J.I.Loch, A.Ściuk, M.Kilichowska, I.Pieróg, W.Łukaszczyk, K.Zimowska, M.Jaskolski (2024),
  Probing the enzymatic activity and maturation process of the EcAIII Ntn-amidohydrolase using local random mutagenesis.
  Acta Biochim. Polon. 72, 01. DOI: 10.3389/abp.2024.12299
• J.Sliwiak, P.Worsztynowicz, K.Pokrywka, M.Grzechowiak, J.I.Loch, M.Jaskolski (2024),
  Biochemical characterization of L-asparaginase isoforms from Rhizobium etli - the boosting effect of zinc.
  Frontiers Chem. 12:1373312. DOI: 10.3389/fchem.2024.1373312
• K.Pokrywka, P.Worsztynowicz, J.Sliwiak, M.Grzechowiak, J.I.Loch, M.Ruszkowski, M.Gilski, M.Jaskolski (2024),
  Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV.
  Frontiers Chem. 12:1381032. DOI: 10.3389/fchem.2024.1381032
• A.Sciuk, K.Wator, I.Staron, P.Worsztynowicz, K.Pokrywka, M.Kilichowska, K.Pietruszewska, Z.Mazurek, A.Skalniak, K.Lewandowski, M.Jaskolski, J.I.Loch, M.Surmiak (2024),
  Substrate affinity is not crucial for therapeutic L-asparaginases: antileukemic activity of novel bacterial enzymes.
  Molecules 29, 2272. DOI: 10.3390/molecules29102272
• A.Wlodawer, Z.Dauter, J.Lubkowski, J.Loch, D.Brzezinski, M.Gilski, M.Jaskolski (2024),
  Towards a dependable dataset of structures for L-asparaginase research.
  Acta Cryst. D80, 506-527. DOI: 10.1107/S2059798324005461

Proteases/inhibitors

• M.Kozak, E.Kozian, Z.Grzonka, M.Jaskolski:
  Crystallization and preliminary crystallographic studies of a new crystal form of papain from Carica papaya.
  Acta Biochim. Polon. 44, 601-606 (1997). [PubMed]
• M.Kozak, E.Kozian, Z.Grzonka, M.Jaskolski:
  Crystallization and Preliminary Crystallographic Studies of a Covalent Complex Between Papain and an Oxirane-Based Inhibitor.
  In: Peptides 1996, eds. R.Ramage and R.Epton. The European Peptide Society, 551-552 (1998).
• C.Czaplewski, Z.Grzonka, M.Jaskolski,F.Kasprzykowski, M.Kozak, E.Politowska, J.Ciarkowski:
  Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?
  Biochim. Biophys. Acta 1431, 290-305 (1999). [PubMed]
• M.Kozak, E.Jankowska, R.Janowski, Z.Grzonka, A.Grubb, M.Alvarez-Fernandez, M.Abrahamson, M.Jaskolski:
  Expression of a selenomethionyl derivative and preliminary crystallographic studies of human cystatin C.
  Acta Cryst. D55, 1939-1942 (1999). [PubMed]
• Z.Grzonka, E.Jankowska,F.Kasprzykowski, R.Kasprzykowska, L.Lankiewicz, W.Wiczk, E.Wieczerzak,J.Ciarkowski, P.Drabik, R.Janowski, M.Kozak, M.Jaskolski, A.Grubb:
  Structural studies of cysteine proteases and their inhibitors.
  Acta Biochim. Polon. 48, 1-20 (2001). [PDF]
• J.Otlewski, M.Jaskolski, O.Buczek, T.Cierpicki, H.Czapinska, D.Krowarsch, A.O.Smalas, D.Stachowiak, A.Szpineta, M.Dadlez:
  Structure-function relationship of serine protease - protein inhibitor interaction.
  Acta Biochim. Polon. 48, 419-428 (2001). [PDF]
• R.Janowski, G.Bujacz, D.Gerlach, M.Jaskolski (2002),
  Crystallization and preliminary crystallographic studies of Streptococcus pyogenes cysteine protease precursor.
  Acta Cryst. D58, 723-726. [PubMed]
• R.Janowski, M.Kozak, E.Jankowska, Z.Grzonka, M.Jaskolski (2004),
  Two polymorphs of a covalent complex between papain and a diazomethylketone inhibitor.
  J. Peptide Res. 64, 141-150. [PubMed]
• A.Ljunggren, I.Redzynia, M.Alvarez-Fernandez, M.Abrahamson, J.S.Mort, J.Krupa, M.Jaskolski, G.Bujacz (2007),
  Crystal structure of the parasitic protease inhibitor chagasin in complex with a host target cysteine protease.
  J. Mol. Biol. 371, 137-153. [PubMed]
• I.Redzynia, A.Ljunggren, M.Abrahamson, J.S.Mort, J.Krupa, M.Jaskolski, G.Bujacz (2008),
  Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B.
  J. Biol. Chem. 283, 22815-22825. [PubMed]
• I.Redzynia, A.Ljunggren, A.D.Bujacz, M.Abrahamson, M.Jaskolski, G.D.Bujacz (2009),
  Crystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteases.
  FEBS J. 276, 793-806. [PubMed]
• M.Jaskolski (2011),
  A new piece in the 3D jigsaw of malaria parasite.
  Structure 19, 901-902. [PubMed]
• S.Krzywda, M.Jaskolski, K.Rolka, M.Stawikowski (2014),
  Structure of proteolytically resistant analog of [NLys]5SFTI-1 in complex with trypsin: evidence for the direct participation of the Ser214 carbonyl group in serine protease mediated proteolysis.
  Acta Cryst. D70, 668-675. [PubMed]
• E.Kopera, W.Bal, M.Lenarcic Zivkovic, A.Dvornyk, B.Kludkiewicz, K.Grzelak, I.Zhukov, W.Zagorski-Ostoja, M.Jaskolski, S.Krzywda (2014),
  Atomic Resolution Structure of a Protein Prepared by Non-Enzymatic His-Tag Removal. Crystallographic and NMR Study of GmSPI-2 Inhibitor.
  PLoSOne 9, e106936, 1-11. [PubMed]

3D Domain swapping

• R.Janowski, M.Kozak, E.Jankowska, Z.Grzonka, A.Grubb, M.Abrahamson, M.Jaskolski:
  Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping.
  Nature Struct. Biol. 8, 316-320 (2001). [PubMed]
• M.Jaskolski:
  3D Domain swapping, protein oligomerization, and amyloid formation.
  Acta Biochim. Polon. 48, 807-827 (2001). [PDF]
• P.P.Liberski, M.Jaskolski (2002),
  Prion diseases: a dual view of the prion hypothesis as seen from a distance. Dedicated to Dr. Carleton Gajdusek on the occasion of his 80th birthday.
  Acta Neurobiol. Exp. 62, 197-226. [PubMed]
• M.Jaskolski, P.P.Liberski (2002),
  Kurt Wuthrich - co-winner of the Nobel Prize in Chemistry, 2002.
  Acta Neurobiol. Exp. 62, 288-289.
• M.Nilsson, X.Wang, S.Rodziewicz-Motowidlo, R.Janowski, V.Lindstrom, P.Onnerfjord, G.Westermark, Z.Grzonka, M.Jaskolski, A.Grubb (2004),
  Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C use of engineered disulfide bridges, antibodies and carboxymethylpapain to stabilize the monomeric form of cystatin C.
  J. Biol. Chem. 279, 24236-24245. [PubMed]
• R.Janowski, M.Abrahamson, A.Grubb, M.Jaskolski (2004),
  3D Domain-Swapped Dimers of N-Truncated Human Cystatin C.
  J. Mol. Biol. 341, 151-160. [PubMed]
• P.P.Liberski, M.Jaskolski, P.Brown (2004),
  Gerstmann-Straussler-Scheinker disease. II. An effect of GSS mutation on PRP structure.
  Folia Neuropathol. 42, 140-152. [PubMed]
• R.Janowski, M.Kozak, M.Abrahamson, A.Grubb, M.Jaskolski (2005),
  3D Domain-swapped human cystatin C with amyloid-like intermolecular b-sheets.
  Proteins: Structure Function, and Bioinformatics 61, 570-578. [PubMed]
• M.Jaskolski, A.Grubb (2005),
  Cystatin C. In: Amyloid proteins: The Beta Sheet Conformation and Disease Vol. 2 (Ed. J.D.Sipe).
  Wiley-VCH Verlag, Weinheim.
• S.Rodziewicz-Motowidlo, M.Wahlbom, X.Wang, J.Lagiewka, R.Janowski, M.Jaskolski, A.Grubb, Z.Grzonka (2006),
  Checking the conformational stability of cystatin C and its L68Q variant by molecular dynamics studies: Why is the L68Q variant amyloidogenic?
  J. Struct. Biol. 154, 68-78. [PubMed]
• E.Levy, M.Jaskolski, A.Grubb (2006),
  Cerebral Cystatin C amyloid Angiopathy
  Brain Pathol. 16, 6-7. [PubMed]
• S.Giannini, A.Sanders, M.Jaskolski, A.Grubb, R.A.Staniforth (2006),
  Cystatins: 3D Domain Swapping and Amyloid Angiopathy. A General Mechanism for the Formation of Amyloid Fibrils? In: Human Stefins and Cystatins (Molecular Anatomy and Physiology of Proteins). (Ed. E.Zerovnik).
  Nova Science Publishers, Inc.
• M.Jaskolski (2007),
  Three-dimensional domain swapping and its relevance to conformational diseases. In: Evolving Methods for Macromolecular Crystallography. (Eds. R.J.Read, J.L.Sussman).
  Springer.
• M.Wahlbom, X.Wang, V.Lindstrom, E.Carlemalm, M.Jaskolski, A.Grubb (2007),
  Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.
  J. Biol. Chem. 281, 18318-18326. [PubMed]
• R.Kolodziejczyk, K.Michalska, A.Hernandez-Santoyo, M.Wahlbom, A.Grubb, M.Jaskolski (2010),
  Crystal structure of human cystatin C stabilized against amyloid formation.
  FEBS J. 277, 1726-1737. [PubMed]
• M.Orlikowska, E.Jankowska, R.Kolodziejczyk, M.Jaskolski, A.Szymanska (2010),
  Hinge-loop mutation can be used to control 3D domain swapping and amyloidogenesis of human cystatin C.
  J. Struct. Biol. 173, 406-413. [PubMed]
• M.Jaskolski (2011),
  3D Domain swapping - implications for conformational disorders and ways of control.
  BioTechnologia 92, 34-44. [PDF]
• M.Jaskolski (2012),
  3D Domain swapping. In: Encyclopedia of Biophysics (G.C.K. Roberts ed.). Springer. [Read]
• K.Michalska, M.Kowiel, L.Bigelow, M.Endres, M.Gilski, M.Jaskolski, A.Joachimiak (2020),
  3D domain swapping in the TIM barrel of the subunit of Streptococcus pneumoniae tryptophan synthase.
  Acta Cryst. D76, 166-175. [OpenAccess]
• L.H.Tran, A.Urbanowicz, M.Jasinski, M.Jaskolski, M.Ruszkowski (2021),
  3D Domain swapping dimerization of the receiver domain of cytokinin receptor CRE1 from Arabidopsis thaliana and Medicago truncatula.
  Frontiers Plant Sci. 12, 756341. [OpenAccess]
• E.Ilowska, J.Barciszewski, M.Jaskolski, A.Molinski, M.Kozak, A.Szymanska (2022),
  Identification of a steric zipper motif in the amyloidogenic core of human cystatin C and its use for the design of self-assembling peptides.
  Int. J. Mol. Sci. 23, 5800. [OpenAccess]

Protein structure at high resolution

• H.Czapinska, J.Otlewski, Sz.Krzywda, G.M.Sheldrick, M.Jaskolski:
  High Resolution Structure of Bovine Pancreatic Trypsin Inhibitor with Altered Binding Loop Sequence.
  J. Mol. Biol. 295, 1237-1249 (2000). [PubMed]
• A.Addlagatta, H.Czapinska, Sz.Krzywda, J.Otlewski, M.Jaskolski:
  Ultrahigh-resolution structure of a BPTI mutant.
  Acta Cryst. D57, 649-663 (2001). [PubMed]
• M.Jaskolski, A.Addlagatta:
  Protein Structure Dissected at Ultra High Resolution.
  In: Methods in Macromolecular Crystallography. D.Turk, L.Johnson eds. IOS Press (2001).
• R.Thaimattam, E.Tykarska, A.Bierzynski, G.M.Sheldrick, M.Jaskolski (2002),
  Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination.
  Acta Cryst. D58, 1448-1461. [PubMed]
• R.Thaimattam, M.Jaskolski (2004),
  Synchrotron radiation in atomic-resolution studies of protein structure.
  J. Alloys Comp. 362, 12-20.
• W.Bialek, Sz.Krzywda, M.Jaskolski, A.Szczepaniak (2009),
  Atomic-resolution structure of reduced cyanobacterial cytochrome c6 with an unusual sequence insertion.
  FEBS J. 276, 4426-4436. [PubMed]
• M.Jaskolski (2013),
  High resolution macromolecular crystallography.
  In: Advancing Methods for Biomolecular Crystallography. R.Read, A.G.Urzhumtsev, V.Y.Lunin eds. pp. 259-275, Springer.
• P.Zatwarnicki, J.Barciszewski, S.Krzywda, M.Jaskolski, P.Kolesinski, A.Szczepaniak (2013),
  Cytochrome c6B of Synechococcus sp. WH 8102 - crystal structure and basic properties of novel c6-like family representative.
  Biochem. Biophys. Res. Commun. 443, 1131-1135. [PubMed]
• W.Bialek, S.Krzywda, P.Zatwarnicki, M.Jaskolski, P.Kolesinski, A.Szczepaniak (2014),
  Insights into the relationship between the haem-binding pocket and the redox potential of c6 cytochromes: four atomic resolution structures of c6 and c6-like proteins from Synechococcus sp. PCC 7002.
  Acta Cryst. D70, 2823-2832. [PubMed]
• M.Jaskolski (2016),
  Structure refinement at atomic resolution. In: Protein Crystallography Methods and Protocols. Vol. in Methods in Molecular Biology 1607 (A.Wlodawer, Z.Dauter, M.Jaskolski eds.), pp. 549-563. Springer. [PubMed]

Nucleic acids

• M.Jaskolski, W.Krzyzosiak, H.Sierzputowska-Gracz, M.Wiewiorowski:
  Comparative Structural Analysis of Cytidine, Ethenocytidine and Their Protonated Salts. I. Crystal and Molecular Structure of Ethenocytidine.
  Nucleic Acids Res. 9, 5423-5442 (1981). [PubMed]
• M.Wiewiorowski, M.Jaskolski, H.Sierzputowska-Gracz, W.J.Krzyzosiak (1981),
  The Comparative Studies of the Structure of Neutral and Cationic Forms of Ethenocytidine and Its Parent Nucleoside.
  In: Nucleosides, Nucleotides and Their Biological Applications. Proc. 4th Int. Round Table, Antwerp, 1981, ed. F.C.Alderweireldt, E.L.Esman, 99-123.
• M.Jaskolski (1982),
  Comparison of Molecular Dimensions and Intermolecular Interactions of Adenosine, Ethenoadenosine and Their Hydrochlorides.
  In: Proceedings, 4th Symposium on Organic Crystal Chemistry, Poznan-Kiekrz, 1982. ed. Z.Kaluski, UAM Poznan, 221-245.
• W.Krzyzosiak, M.Jaskolski, H.Sierzputowska-Gracz, M.Wiewiorowski:
  Comparative Structural Analysis of Cytidine, Ethenocytidine and Their Protonated Salts. II. IR Spectral Studies.
  Nucleic Acids Res. 10, 2741-2753, (1982). [PubMed]
• M.Jaskolski:
  Ethenoadenosine. Acta Cryst. B38, 3171-3174 (1982).
• M.Jaskolski:
  Crystal and Molecular Structure of 1,N6-Ethenoadenosine Hydrochloride.
  J. Cryst. Spectr. Res. 14, 45-57 (1984).
• L.Kozerski, H.Sierzputowska-Gracz, W.Krzyzosiak, M.Bratek-Wiewiorowska, M.Jaskolski, M.Wiewiorowski:
  Comparative Structural Analysis of Cytidine, Ethenocytidine and Their Protonated Salts. III. 1H, 13C and 15N NMR Studies at Natural Isotope Abundance.
  Nucleic Acids Res. 12, 2205-2223 (1984). [PubMed]
• M.Jaskolski, M.Alejska:
  Structure of 3-Methylcytidinium Chloride.
  Acta Cryst. C41, 599-602 (1985).
• W.J.Krzyzosiak, M.Wiewiorowski, M.Jaskolski (1986),
  Chemical Modification of Adenine and Cytosine Residues with Chloroacetaldehyde at the Nucleoside and tRNA Level: the Structural Effect of Chloroacetaldehyde Modification.
  In: The Role of Cyclic Nucleic Acid Adducts in Carcinogenesis and Mutagenesis. Int. Agency for Res. on Cancer, 75-81.
• M.Wiewiorowski, M.D.Bratek-Wiewiorowska, M.Alejska, A.Perkowska, W.Krzyzosiak, M.Jaskolski, U.Rychlewska:
  The Influence of Counter Anions on the Conformations and Molecular Interactions of Protonated Nucleosides.
  Chem. Scripta 26, 229-240 (1986).
• M.Jaskolski, B.Skalski, D.A.Adamiak, R.W.Adamiak:
  Structure of N-(2-Amino-6-purinyl)pyridinium Chloride Dihydrate.
  Acta Cryst. C43, 2110-2113 (1987).
• M.Jaskolski, M.Wiewiorowski:
  Structure of 3-Methylcytidinium Nitrate.
  Acta Cryst. C43, 89-92 (1987).
• M.Jaskolski, B.Skalski, D.A.Adamiak:
  Structure of N,N'-(2,4-Pyrimidinediyl)dipyridinium Dichloride Monohydrate. Dedicated to Professor Maciej Wiewiorowski on the occasion of his 70th birthday.
  Acta Cryst. C44, 1409-1412 (1988).
• M.Jaskolski:
  Structure of Cytidinium Dihydrogenphosphate.
  Acta Cryst. C45, 85-89 (1989).
• M.Jaskolski:
  Structure of 2'-Deoxycytidinium Dihydrogenphosphate.
  Acta Cryst. C47, 153-156 (1991).
• M.Jaskolski, B.Skalski, D.A.Adamiak:
  Structure of 2-(Pyridinium-1)-4-(4'-formylbutadien-1',3'-yl)amino-5-fluoropyrimidine Chloride Trihydrate.
  Acta Cryst. C47, 1009-1012 (1991).
• M.Gilski, E.Bartoszak, M.Jaskolski:
  Structure of 3,N4-Ethenocytidinium Dihydrogenphosphate.
  Acta Cryst. C47, 1460-1463 (1991).
• M.D.Bratek-Wiewiorowska, M.Alejska, N.Malinowska, J.Sarzynska, M.Figlerowicz, E.Utzig, W.Zielenkiewicz, M.Jaskolski, M.Wiewiorowski:
  Crystal Engineering of Cytidine and Deoxycytidine Sulfates. I. Preparation and Unusual Properties.
  Tetrahedron 48, 4893-4904 (1992).
• M.Jaskolski, A.Myszka, M.Gilski, M.Alejska, N.Malinowska:
  Base Pairing of Hemiprotonated 2'-Deoxycytidine. Crystal and Molecular Structure of (Hydrated) 2'-Deoxycytidine Hemiperchlorate.
  Pol. J. Chem. 67, 745-753 (1993).
• M. Gilski, M. Jaskolski:
  Crystal and Molecular Structure of Cytidinium Sulfate.
  Pol. J. Chem. 67, 1841-1850 (1993).
• M.Jaskolski, M.Gdaniec, M.Gilski, M.Alejska, M.D.Bratek-Wiewiorowska:
  Crystal Structure of 2'-deoxycytidine hemidihydrogenphosphate reveals C+.C base pairs and tight, hydrogen-bonded (H2PO4)inf columns.
  J. Biomol. Struct. Dyn. 11, 1-20 (1994). [PubMed]
• M.Jaskolski, M.Wiewiorowski:
  Isomorphism, solid state transformations, and disorder in the crystal structures of cytidinium and 2'-deoxycytidinium salts.
  In: Organic Crystal Chemistry, ed. D.Jones. Oxford Univ. Press, 203-217 (1994).
• M.Jakob, R.Kolodziejczyk, M.Orlowski, Sz.Krzywda, A.Kowalska, J.Dutko-Gwozdz, T.Gwozdz, M.Jaskolski, A.Ozyhar (2007),
  Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain.
  Nucleic Acids Res. 35, 2705-2718. [PubMed]
• K.Brzezinski, A.Brzuszkiewicz, M.Dauter, M.Kubicki, M.Jaskolski, Z.Dauter (2011),
  High regularity of Z-DNA revealed by ultra high-resolution crystal structure at 0.55 A.
  Nucleic Acids Res. 39, 6238-6248. [PDF]
• P.Drozdzal, K.Michalska, R.Kierzek, L.Lomozik, M.Jaskolski (2012),
  Structure of an RNA/DNA dodecamer corresponding to the HIV-1 polypurine tract at 1.6 A resolution.
  Acta Cryst. D68, 169-175. [PubMed]
• P.Drozdzal, M.Gilski, R.Kierzek, L.Lomozik, M.Jaskolski (2013),
  Ultrahigh-resolution crystal structures of Z-DNA in complex with Mn2+ and Zn2+ ions.
  Acta Cryst. D69, 1180-1190. [PubMed]
• P.Drozdzal, M.Gilski, R.Kierzek, L.Lomozik, M.Jaskolski (2015),
  High-resolution crystal structure of Z-DNA in complex with Cr3+ cations.
  J. Biol. Inorg. Chem. 20,596-602. [PubMed]
• P.Drozdzal, M.Gilski, M.Jaskolski (2021) Crystal structure of Z-DNA in complex with the polyamine putrescine and potassium cations determined at ultrahigh resolution. Acta Cryst. B77, 331-338. [OpenAccess]

Biogenic polyamines

• M.Jaskolski, M.Alejska, M.Wiewiorowski:
  Crystal and Molecular Structure of Putrescinium Hydrogen Phosphate Dihydrate.
  J. Cryst. Spectr. Res. 16, 31-39 (1986).
• M.D.Bratek-Wiewiorowska, M.Alejska, A.Perkowska, M.Wiewiorowski, M.Jaskolski, F.Cramer (1986),
  Comparative Structural Analysis of the Salts of Putrescine (Pu),Spermidine (Spd) and Spermine (Sp) in the Aspect of Their Interactions with Nucleic Acids. III. Hydrogen Bonding Systems in Crystals of Hydrochlorides and Hydrated Phosphates of Pu, Spd and Sp.
  Bull. Acad. Pol. Sci. Chim. 34, 229-249.
• M.Jaskolski, M.Wiewiorowski (1986),
  Structural Investigations of Biogenic Polyamines Salts: Molecular and Crystal Structures of Putrescinium and Sperminium Nitrates.
  In Proceedings, Pre-Meeting Symposium on Organic Crystal Chemistry, Poznan-Rydzyna, August 1986. ed. Z.Kaluski, UAM Poznan, 205-219.
• M.Jaskolski:
  Structure of Putrescinium Dinitrate.
  Acta Cryst. C43, 1761-1763 (1987).
• M.Jaskolski:
  Structure of Sperminium Tetranitrate.
  Acta Cryst. C43, 1375-1378 (1987).
• M.D.Bratek-Wiewiorowska, M.Alejska, M.Figlerowicz, J.Barciszewski, M.Wiewiorowski, M.Jaskolski:
  Interaction of polyamines, their protonated salts and metal complexes with nucleic acid fragments.
  Pure Appl. Chem. 59, 407-414 (1987).
• M.Jaskolski, I.Olovsson:
  Structure of Putrescinium Dinitrate at Three Low Temperatures (30, 120 and 275K).
  Acta Cryst. B45, 78-85 (1989).
• E.Bartoszak, M.Jaskolski:
  Structure of Putrescinium Dihydrogendiphosphate.
  Acta Cryst. B46, 2158-2160 (1990).
• E.Bartoszak-Adamska, M.Figlerowicz, M.Wiewiorowski, T.Gustafsson, I.Olovsson, M.Jaskolski:
  The influence of (O,N)-deuteration on the crystal and molecular structure, thermal stability and spectroscopic properties of 1,3-propanediammonium hydrogenphosphate monohydrate.
  Pol. J. Chem. 74, 393-408 (2000).

Alkaloids

• D.Pyzalska, M.Jaskolski, T.Borowiak, J.Wolinska-Mocydlarz:
  The Structure of Dehydromultiflorine Perchlorate.
  Acta Cryst. B36, 1685-1687 (1980).
• B.Golankiewicz, M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz:
  Hydrogenation Products of Some Cinchona Alkaloids. Part VI. Crystal Structure of alpha-1',2',3',4',10,11-Hexahydrocinchonine Dihydrochloride. Absolute Configuration around the 4' Chiral Center of Hexahydrocinchonines and Their Derivatives.
  Pol. J. Chem. 55, 2279-2287 (1981).
• P.Dokurno, M.Jaskolski, Z.Kosturkiewicz, D.Matecka, M.D.Rozwadowska:
  Structure of (-)-Narcotine Hemiacetal.
  Acta Cryst. C47, 1012-1014 (1991).

Hormones

• A.Anthony, M.Jaskolski, A.Nangia, G.R.Desiraju:
  5-beta-Andrastan-3,17-dione.
  Acta Cryst. C54, 1898-1900 (1998).
• A.Anthony, M.Jaskolski, A.Nangia, G.R.Desiraju:
  17-Ethylenedioxyandrost-4-ene-3,6-dione and 17-Ethylenedioxyandrost-1,4-diene-3,6-dione.
  Acta Cryst. C54, 1894-1898 (1998).
• A.Anthony, M.Jaskolski, A.Nangia (1999),
  Androst-4-ene-3,6,17-trione.
  Acta Cryst. C55, 787-789.
• J.Biesiadka, M.M.Sikorski, G.Bujacz, M.Jaskolski (1999),
  Crystallization and preliminary X-ray structure determination of Lupinus luteus PR10 protein.
  Acta Cryst. D55, 1925-1927. [PubMed]
• J.Biesiadka, G.Bujacz, M.M.Sikorski, M.Jaskolski (2002),
  Crystal structures of two homologous pathogenesis-related proteins from yellow lupine.
  J. Mol. Biol. 319, 1223-1234. [PubMed]
• G.D.Bujacz, O.Pasternak, Y.Fujimoto, Y.Hashimoto, M.M.Sikorski, M.Jaskolski (2003),
  Crystallization and preliminary crystallographic studies of cytokinin-specific binding protein from mung bean.
  Acta Cryst. D59, 522-525. [PubMed]
• R.Kolodziejczyk, M.Kochman, G.Bujacz, P.Dobryszycki, A.Ozyhar, M.Jaskolski (2003),
  Crystallization and preliminary crystallographic studies of Juvenile Hormone Binding Protein from Galleria mellonella hemolymph.
  Acta Cryst. D59, 519-521. [PubMed]
• O.Pasternak, J.Biesiadka, R.Dolot, G.Bujacz, M.M.Sikorski, M.Jaskolski (2005),
  Crystal structure of a yellow lupine pathogenesis-related PR-10 protein belonging to a novel subclass.
  Acta Cryst. D61, 99-107. [PubMed]
• O.Pasternak, G.D.Bujacz, Y.Fujimoto, Y.Hashimoto, F.Jelen, J.Otlewski, M.M.Sikorski, M.Jaskolski (2006),
  Crystal structure of Vigna radiata Cytokinin-Specific Binding Protein in Complex with Zeatin.
  The Plant Cell 18, 2622-2634. [PDF]
• R.Kolodziejczyk, G.Bujacz, M.Jakob, A.Ozyhar, M.Jaskolski, M.Kochman (2008),
  Insect juvenile hormone binding protein exhibits ancestral fold present in human lipid binding proteins.
  J. Mol. Biol. 377, 870-881. [PubMed]
• H.Fernandes, O.Pasternak, G.Bujacz, A.Bujacz, M.M.Sikorski, M.Jaskolski (2008),
  L. luteus pathogenesis-related protein as a reservoir for cytokinins.
  J. Mol. Biol. 378, 1040-1051. [PubMed]
• H.Fernandes, M.Konieczna, R.Kolodziejczyk, G.Bujacz, M.Sikorski, M.Jaskolski (2008),
  Crystallization and preliminary crystallographic studiem of Hyp-1, a St John's wort protein implicated in the biosynthesis of hypericin.
  Acta Cryst. F64, 405-408. [PubMed]
• H.Fernandes, G.Bujacz, A.Bujacz, F.Jelen, M.Jasinski, P.Kachlicki, J.Otlewski, M.Sikorski, M.Jaskolski (2009),
  Cytokinin-induced structural adaptatability of a Lupinus luteus PR-10 protein.
  FEBS J. 276, 1596-1609. [PubMed]
• K.Michalska, H.Fernandes, M.Sikorski, M.Jaskolski (2010),
  Crystal structure of Hyp-1, a St John's wort protein with implication in the biosynthesis of hypericin.
  J. Struct. Biol. 169, 161-171. [PubMed]
• M.Jaskolski (2009),
  Bialka PR-10 jako rezerwuar ligandow w komorce roslinnej.
  Postepy biol. kom. 36, 59-68.
• A.Pietrzyk, A.Bujacz, M.Lochynska, M.Jaskolski, G.Bujacz (2011),
  Isolation, purification, crystallization and preliminary X-ray studies of two 30 kDa proteins from silkworm haemolymph.
  Acta Cryst. F67, 372-376. [PubMed]
• A.Wojtkowiak, K.Witek, J.Hennig, M.Jaskolski (2012),
  Two high-resolution crystal structures of potato endo-1,3-glucanase reveal domain flexibility with implications for substrate binding.
  Acta Cryst. D68, 713-723. [PubMed]
• A.J.Pietrzyk, S.Panjikar, A.Bujacz, J.Mueller-Dieckmann, M.Lochynska, M.Jaskolski, G.Bujacz (2012),
  High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxification.
  Acta Cryst. D68, 1140-1151. [PubMed]
• A.Wojtkowiak, K.Witek, J.Hennig, M.Jaskolski (2013),
  Crystal structures of active-site mutant of plant 1,3-beta-glucanase in complex with oligosaccharide products of hydrolysis.
  Acta Cryst. D69, 52-62. [PubMed]
• H.Fernandes, K.Michalska, M.Sikorski, M.Jaskolski (2013),
  Structural and functional aspects of PR-10 proteins.
  FEBS J. 280, 1169-1199. [PDF]
• A.J.Pietrzyk, A.Bujacz, J.Mueller-Dieckmann, M.Lochynska, M.Jaskolski, G.Bujacz (2013),
  Two crystal structures of Bombyx mori lipoprotein 3 - structural characterization of a new 30-kDa lipoprotein family member.
  PLoSOne 8, e61303, 1-10. [OpenAccess]
• A.J.Pietrzyk, M.Jaskolski, G.Bujacz (2013),
  Structural studies of juvenile hormone binding proteins. In: Juvenile Hormones and Juvenoids: Modeling Biological Effects and Environmental Fate (J.Deviller, ed.). pp 291-309. CRC Press.
• M.Ruszkowski, K.Brzezinski, R.Jedrzejczak, M.Dauter, Z.Dauter, M.Jaskolski, M.Sikorski (2013),
  M. truncatula histidine-containing phosphotransfer protein: structural insight into cytokinin transduction pathway in plants.
  FEBS J. 280, 3709-3720. [PubMed]
• J.Kosuth, D.Hrehorova, M.Jaskolski, E.Cellarova (2013),
  Stress-induced expression and structure of the putative gene hyp-1 for hypericin biosynthesis.
  Plant Cell Tiss. Organ Cult. 114, 207-2016.
• A.J.Pietrzyk, A.Bujacz, J.Mueller-Dieckmann, M.Lochynska, M.Jaskolski, G.Bujacz (2013),
  Crystallographic identification of an unexpected protein complex in silkworm hemolymph.
  Acta Cryst. D69, 2353-2364. [PubMed]
• M.Ruszkowski, K.Szpotkowski, M.Sikorski, M.Jaskolski (2013),
  The landscape of cytokinin binding by a plant nodulin.
  Acta Cryst. D69, 2365-2380. [PubMed]
• M.Chwastyk, M.Jaskolski, M.Cieplak (2013),
  Structure-based thermodynamic and mechanical stability of plant PR-10 proteins.
  FEBS J. 281, 416-429. [PubMed]
• M.Ruszkowski, J.Sliwiak, A.Ciesielska, J.Barciszewski, M.Sikorski, M.Jaskolski (2014),
  Specific binding of gibberellic acid by Cytokinin-Specific Binding Proteins: a new aspect of plant hormone-binding proteins with PR-10 fold.
  Acta Cryst. D70, 2032-2041. [PubMed]
• A.J.Pietrzyk, A.Bujacz, M.Lochynska, M.Jaskolski, G.Bujacz (2014),
  Crystal structure of Bombyx mori lipoprotein 6: comparative structural analysis of the 30-kDa lipoprotein family.
  PLoSOne 9, e108761, 1-10. [OpenAccess]
• J.Sliwiak, R.Dolot, K.Michalska, K.Szpotkowski, G.Bujacz, M.Sikorski, M.Jaskolski (2016),
  Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein.
  J. Struct. Biol. 193, 55-66. [PubMed]
• J.Sliwiak, Z.Dauter, M.Jaskolski (2016),
  Crystal structure of Hyp-1, a Hypericum perforatum PR-10 protein, in complex with melatonin.
  Frontiers Plant Sci. 7, 668. [OpenAccess]
• J.Sliwiak, M.Sikorski, M.Jaskolski (2018),
  PR-10 proteins as potential mediators of melatonin-cytokinin cross-talk in plants: crystallographic studies of LlPR-10.2B isoform from yellow lupine.
  FEBS J. 285, 1907-1922. [PubMed]

Small and large biologicals - other

• A.Gzella, L.Zaprutko, U.Wrzeciono, M.Jaskolski (1987),
  Triterpenoids. III. Structure of 3-Acetoxy-11-oxo-18-olean-12-ene-28-oic Acid Methyl Ester, C33H50O5.
  Acta Cryst. C43, 759-762.
• M.Jaskolski (1987),
  Structure of 1,2-Dipiperidinoethane Mono-N-oxide Trihydrate.
  Acta Cryst. C43, 2391-2393.
• MD.Bratek-Wiewiorowska, A.Perkowska, M.Alejska, M.Figlerowicz, K.Langowska, M.Jaskolski, M.Wiewiorowski (1987),
  Variety of Molecular Interactions of Phosphates and Their Biological Significance.
  In: Biophosphates and Their Analogues - Synthesis, Structure, Metabolism and Activity, edited by K.S. Bruzik and W.J.Stec. Elsevir Science Publishers BV, 525-545.
• A.Wojtczak, M.Jaskolski, Z.Kosturkiewicz (1988),
  Structure of Histaminium Dinitrate.
  Acta Cryst. C44, 1779-1781.
• M.Kozak, B.Hayward, D.Borek, D.T.Bonthron, M.Jaskolski (2001),
  Expression, purification and preliminary crystallographic studies of human ketohexokinase.
  Acta Cryst. D57, 586-588 (2001). [PubMed]
• K.Brzezinski, R.Janowski, J.Podkowinski, M.Jaskolski (2001),
  Sequence determination and analysis of S-adenosyl-L-homocysteine hydrolase from yellow lupine (Lupinus luteus).
  Acta Biochim. Polon. 48, 477-483 (2001). [PDF]
• E.Jankowska, M.Gilski, M.Jaskolski, Z.Grzonka, L.Lankiewicz (2002),
  Crystal structure of N-t-butoxycarbonyl-N-methyl-(O-benzyl)-L-tyrosine.
  Acta Cryst. C58, 353-354. [PubMed]
• K.Brzezinski, B.Rogozinski, T.Stepkowski, G.Bujacz, M.Jaskolski (2004),
  Cloning, purification, crystallization and preliminary crystallographic studies of Bradyrhizobium fucosyltransferase NodZ.
  Acta Cryst. D60, 344-346. [PubMed]
• G.Tamulaitiene, S.Grazulis, A.Janulaitis, R.Janowski, G.Bujacz, M.Jaskolski (2003),
  Crystallization and preliminary crystallographic studies of a bifunctional restriction endonuclease Eco57I.
  Biochim. Biophys. Acta 1698, 251-254. [PubMed]
• K.Brzezinski, T.Stepkowski, S.Panjikar, G.Bujacz, M.Jaskolski (2007),
  High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.
  Acta Biochim. Polon. 54, 537-549. [PDF]
• K.Brzezinski, G.Bujacz, M.Jaskolski (2008),
  Purification, crystallization and preliminary crystallographic studies of plant S-adenosylhomocysteine hydrolase (Lupinus luteus).
  Acta Cryst. F64, 671-673. [PubMed]
• M.Tarnawski, Sz.Krzywda, A.Szczepaniak, M.Jaskolski (2008),
  Rational "correction" of the amino acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization.
  Acta Cryst. F64, 870-874. [PubMed]
• O.Cakici, M.Sikorski, T.Stepkowski, G.Bujacz, M.Jaskolski (2008),
  Cloning, expression, purification, crystallization and preliminary X-ray analysis of NodS N-methyltransferase from Bradyrhizobium japonicum WM9.
  Acta Cryst. F64, 1149-1152. [PubMed]
• O.Cakici, M.Sikorski, T.Stepkowski, G.Bujacz, M.Jaskolski (2010),
  Crystal structures of NodS N-methyltransferase from Bradyrhizobium japonicum in ligand-free form and as SAH complex.
  J. Mol. Biol. 404, 874-889. [PubMed]
• M.Tarnawski, Sz.Krzywda, W.Bialek, M.Jaskolski, A.Szczepaniak (2011),
  Structure of RuBisCO chaperone RbcX from the thermophilic cyanobacterium Thermosynechococcus elongatus.
  Acta Cryst. F67, 851-857. [PubMed]
• M.Zarzycki, R.Kolodziejczyk, E.Maciaszczyk, R.Wysocki, M.Jaskolski, A.Dzugaj (2011),
  Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.
  Acta Cryst. D67, 1028-1034. [PubMed]
• K.Brzezinski, Z.Dauter, M.Jaskolski (2012),
  Crystal structures of NodZ 1,6-fucosyltransferase in complex with GDP and GDP-fucose.
  Acta Cryst. D68, 160-168. [PubMed]
• K.Brzezinski, Z.Dauter, M.Jaskolski (2012),
  High-resolution structures of complexes of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus).
  Acta Cryst. D68, 218-231. [PubMed]
• J.Czubinski, J.Barciszewski, M.Gilski, K.Szpotkowski, J.Debski, E.Lampart-Szczapa, M.Jaskolski (2015),
  Crystal structure of conglutin gamma: insight into quaternary structure of 7S basic globulins from legumes.
  Acta Cryst. D71, 224-238. [PubMed]
• T.Manszewski, K.Singh, B.Imiolczyk, M.Jaskolski (2015),
  An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.
  Acta Cryst. D71, 2422-2432. [PubMed]
• J.Barciszewski, J.Wisniewski, M.Jaskolski, D.Rakus, A.Dzugaj (2016),
  T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure.
  Acta Cryst. D72, 536-550. [PubMed]
• T.Manszewski, K.Szpotkowski, M.Jaskolski (2017),
  Crystallographic and SAXS studies of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.
  IUCrJ 4, 271-282. OpenAccess
• K.Brzezinski, J.Czyrko, J.Sliwiak, E.Nalewajko-Sieliwoniuk, M.Jaskolski, B.Nocek, Z.Dauter (2017),
  S-adenosyl-Lhomocysteine hydrolase from a hyperthermophile (Thermatoga maritima) is expressed in Escherichia coli in inactive form - Biochemical and structural studies.
  Int. J. Biol. Macromol. 104, 584-596. PMID: 28629859, DOI:10.1016/j.ijbiomac.2017.06.065 . [PubMed]
• L.L.Kailing, D.Bertinetti, C.E.Paul, T.Manszewski, M.Jaskolski, F.W.Herberg, I.V.Pavlidis (2018),
  S-Adenosyl-L-Homocysteine Hydrolase Inhibition by a Synthetic Nicotinamide Cofactor Biomimetic.
  Front. Microbiol. 9, 505. doi: 10.3389/fmicb.2018.00505 . [PubMed]
• J.Czyrko, M.Jaskolski, K.Brzezinski (2018),
  Crystal structure of S-adenosyl-Lhomocysteine hydrolase from Cytophaga hutchinsonii, a case of combination of crystallographic and non-crystallographic symmetry.
  Croatica Chemica Acta, 91, 153-162. [OpenAccess]
• J.Czyrko, J.Sliwiak, B.Imiolczyk, Z.Gdaniec, M.Jaskolski, K.Brzezinski (2018),
  Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa.
  Sci. Rep. 8, 11334. [OpenAccess]
• M.Grzechowiak, J.Sliwiak, M.Jaskolski, M.Ruszkowski (2020),
  Structural studies of glutamate dehydrogenase (isoform 1) from Arabidopsis thaliana, an important enzyme at the branch-point between carbon and nitrogen metabolism.
  Frontiers in Plant Science 11, 754. [PDF]
• J.Barciszewski, K.Szpotkowski, J.Wisniewski, R.Kolodziejczyk, M.Jaskolski, D.Rakus, A.Dzugaj (2021),
  Structural studies of human muscle FBPase.
  Acta Biochim. Polon. 68, 5-14. [PDF]
• J.I.Loch, J.Barciszewski, J.Sliwiak, P.Bonarek, P.Wrbel, K.Pokrywka, I.G.Shabalin, W.Minor, M.Jaskolski, K.Lewinski (2022),
  New ligand binding sites identified in the crystal structures of beta-lactoglobulin complexes with desipramine.
  IUCrJ 9, 386-398. [OpenAccess]
• M.Grzechowiak, A.Ruszkowska, J.Sliwiak, A.Urbanowicz, M.Jaskolski, M.Ruszkowski (2022),
  New aspects of DNA recognition by group II WRKY transcription factor revealed by structural and functional study of AtWRKY18 DNA binding domain.
  Int. J. Biol. Macromol. 213, 589-601. [OpenAccess]
• P.H.Malecki, B.Imiolczyk, J.Barciszewski, J.Czyrko-Horczak, J.Sliwiak, M.Gawel, K.Wozniak, M.Jaskolski, K.Brzezinski (2022),
  Biochemical and structural insights into an unusual, alkali metal-independent S-adenosyl-L-homocysteine hydrolase from Synechocystis sp. PCC 6803.
  Acta Cryst. D78, 865-882. DOI: https://doi.org/10.1107/S2059798322005605 [OpenAccess]
• J.Wisniewski, J.Barciszewski, J.Turlik, K.Baran, P.Duda, M.Jaskolski, D.Rakus (2022),
  High-resolution crystal structure of muscle phosphoglycerate mutase provides insight into its nuclear import and role.
  Int. J. Mol. Sci. 2022, 23, 13198. DOI: 10.3390/ijms232113198
• L.Dabos, J.E.Raczynska, P.Bogaerts, A.Zavala, D.Girlich, R.Bonnin, L.Dortet, A.Peyrat, P.Retailleau, B.Iorga, M.Jaskolski, Y.Glupczynski, T.Naas (2023),
  Structural and biochemical features of OXA-517: a carbapenem and expanded-spectrum cephalosporin hydrolyzing OXA-48 variant.
  Antimicrobial Agents and Chemotherapy e0109522. DOI: 10.1128/aac.01095-22
• M.Grzechowiak, J.Sliwiak, M.Jaskolski, M.Ruszkowski (2023),
  Structural and functional studies of Arabidopsis thaliana glutamate dehydrogenase isoform 2 demonstrate enzyme dynamics and identify its calcium binding site.
  Plant Physiology and Biochemistry 201, 107895. DOI: 10.1016/j.plaphy.2023.107895

Amidines

• E.Tykarska, M.Jaskolski, Z.Kosturkiewicz:
  Structure of N2-(p-Methoxyphenyl)-N1,N1-penthamethylenebenzamidine.
  Acta Cryst. C42, 740-743 (1986).
• E.Ciszak, M.Gdaniec, M.Jaskolski, J.Oszczapowicz, K.Surma, E.Tykarska, Z.Kosturkiewicz (1986),
  Some aspects of crystal chemistry of amidines.
  In: Proceedings of the Sixth Symposium on Organic Crystal Chemistry, Poznan-Rydzyna 1-4 August 1986. Ed. by Z.Kaluski, 291-298.
• J.Oszczapowicz, E.Tykarska, M.Jaskolski, Z.Kosturkiewicz:
  Structure of N1-Methyl-N1-phenyl-N2-(p-tolyl)benzamidine.
  Acta Cryst. C42, 1816-1818 (1986).
• E.Tykarska, M.Jaskolski, Z.Kosturkiewicz:
  Structure of N2-(m-Chlorophenyl)-N1,N1-pentamethylenebenzamidine.
  Acta Cryst. C42, 208-210 (1986).
• E.Ciszak, M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz:
  Structure of N1,N2-Di(p-tolyl) acetamidine.
  Acta Cryst. C44, 2144-2146 (1988).
• K.Surma, M.Jaskolski, Z.Kosturkiewicz, J.Oszczapowicz:
  Structure of N2-p-Nitrophenylbenzamidine.
  Acta Cryst. C44, 1031-1033 (1988).
• E.Ciszak, M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz, J.Owsianski, E.Tykarska:
  The Structures of Three N1,N1-Dimethyl-N2-p-nitrophenylamidines: Form-, Acet- and 2,2-Dimethylpropionamidine.
  Acta Cryst. C45, 433-438 (1989).
• E.Ciszak, M.Jaskolski, Z.Kosturkiewicz:
  Structure of N1,N1-(3-oxopentamethylene)-N2-phenylacetamidine.
  Acta Cryst. C46, 456-458 (1990).

Liquid crystals

• U.Baumeister, H.Hartung, M.Gdaniec, M.Jaskolski:
  Crystal and Molecular Structure of the Nematogenic Compound 4'-Cyanophenyl-4-n-pentoxybenzoate.
  Mol. Cryst. Liq. Cryst. 69, 119-130, (1981).
• U.Baumeister, H.Hartung, M.Jaskolski:
  The Crystal and Molecular Structure of the Nematogenic Compound 4'-Cyanophenyl-4-n-pentylcyclohexanoate.
  Cryst. Res. and Technol. 17, 153-180, (1982).
• U.Baumeister, H.Hartung, M.Jaskolski:
  The Crystal and Molecular Structure of 4'-Cyanophenyl-4-n-Pentylbenzoate.
  Mol. Cryst. Liq. Cryst. 88, 167-181 (1982).
• U.Baumeister, W.Brandt, H.Hartung, M.Jaskolski:
  Zum Konformationsverhalten substituierter Benzoesaeurephenylester - Molekuel- und Kristallstruktur der nematogenen Verbindung 4-n-Pentoxybenzoesaeure-4'-(b-cyanoethyl)-phenylester.
  J. Prakt. Chem. 325, 742-752 (1983).
• I.Rapthel, H.Hartung, M.Jaskolski:
  Structure of the Nematogenic Compound 5,8-Dihydro-6,7-Dimethyl-1,4-naphtalenediyl Bis(4-ethoxybenzoate), C30H30O6.
  Acta Cryst. C39, 748-750 (1983).
• H.Hartung, U.Baumeister, F.Thielmann, M.Jaskolski:
  Structure of the Nematogenic Compound 6-Hexylamino-1,2,4, 5-tetrazin-3-yl 4-Pentyloxybenzoate, C20H29N5O3.
  Acta Cryst. C40, 482-484 (1984).
• I.Rapthel, H.Hartung, R.Richter, M.Jaskolski:
  Zum konfor4mationsverhalten isomerer Phenylpyrimidine - Molekuel- und Kristallstruktur von 5-Chlor-2-(4-n-hexyloxyphenyl)-pyrimidin.
  J. Prakt. Chem. 325, 489-495 (1984).
• U.Baumeister, H.Hartung, M.Jaskolski:
  The Crystal and Molecular Structure of the Nematogenic Compound 5,8-Dihydro-5,8-methano-1,4-naphtalenediyl-bis(4-ethoxybenzoate).
  Cryst. Res. and Technol. 19, 681-690 (1984).
• U.Baumeister, W.Brandt, H.Hartung, W.Wedler, M.Jaskolski, H.J.Deutscher, R.Frach:
  Conformational Behaviour of the Nematogenic Compound 4-Cyanophenyl-trans-4-[(trans-4-n-butylcyclohexyl)-methyl] cyclohexanoate - Crystal Structure and Theoretical Conformational Analysis.
  Mol. Cryst. Liq. Cryst. 130, 321-336 (1985).
• H.Hartung, U.Baumeister, M.Jaskolski:
  Molekul- und Kristallstruktur der mesogenen Verbindung 4-n-Nonyloxybenzoesaure-4'-(2,2-dicyanethenyl)phenylester.
  Z. Chem. 26 Jg., 32-33 (1986).
• H.Hartung, U.Baumeister, M.Jaskolski, A.Madicke, A.Wiegeleben:
  Crystal Structure and Thermal Phase Behaviour of 2,3-Dicyano-4-n-hexyloxyphenyl-trans-4-n-heptylcyclohexanoate.
  Cryst. Res. and Technol. 21, 103-110 (1986).
• G.Winter, H.Hartung, M.Jaskolski:
  Crystal and Molecular Structure of Two Isostructural 2,5-Diphenyl Pyrimidines.
  Mol. Cryst. Liq. Cryst. 149, 17-27 (1987).
• G.Winter, H.Hartung, W.Brandt, M.Jaskolski:
  Crystal Structure and Conformational Behavior of Smectogenic 2-Phenyl-5-(4-n-pentoxyphenyl)Pyrimidine.
  Mol. Cryst. Liq. Cryst. 150b, 289-300 (1987).
• R.Krieg, H.-J.Deutscher, U.Baumeister, H.Hartung, M.Jaskolski:
  Liquid Crystalline 4-(4-Cyanocyclohexyl)cyclohexyl Esters. Crystal and Molecular Structure of Smectogenic trans-4-(cis-4-Cyanocyclohexyl)cyclohexyl trans-4-n-Heptylcyclohexanoate.
  Mol. Cryst. Liq. Cryst. 166, 109-122 (1989).

Complexes

• A.Wojtczak, M.Jaskolski, Z.Kosturkiewicz:
  Bis(5-(2-ammonioethyl)imidazole-N3)tetrakis(isothiocyanato) nickel(II), (Ni(C5H10N3)2(NCS)4).
  Acta Cryst. C39, 545-547 (1983).
• L.Lomozik, A.Wojciechowska, M.Jaskolski:
  Complex Formation Studies of Copper(II) and Zinc(II) with Asparagine and Aspartic Acid in Aqueous Solution.
  Monatsh. Chem. 114, 1185-1188 (1983).
• A.Wojtczak, M.Jaskolski, Z.Kosturkiewicz:
  ab,cf-Bis(4-(2-aminoethyl)imidazole-N3,N8)-de-bis(isothiocyanato)nickel(II).
  Acta Cryst. C41, 1752-1755 (1985).
• A.Wojtczak, M.Jaskolski, Z.Kosturkiewicz:
  Structure of catena-Bis[4-(2-aminoethyl)imidazole-N3,N8]-mi-chloro-copper(II) Chloride Dihydrate.
  Acta Cryst. C43, 645-648 (1987).
• A.Wojtczak, M.Jaskolski:
  Structure of Histaminium Tetraaquadisulfatomanganate(II) Monohydrate.
  Acta Cryst. C45, 30-33 (1989).
• A.Wojtczak, M.Jaskolski, T.Ossowski:
  Structure of [10-(2-Aminophenyl)-5-methyl-1,5,9-triaza-9-decene-N,N',N'',N''']iodocopper(II) Iodide.
  Acta Cryst. C46, 1918-1920 (1990).
• A.Wojtczak, E.Szlyk, M.Jaskolski, E.Larsen:
  An Optically Active Nickel(II) Schiff Base Coordination Compound N,N'-(1R,2R)-(-)-1,2-Cyclohexylenebis(salicylideneiminato)nickel(II).
  Acta Chem. Scand. 51, 274-278 (1997).
• E.Szlyk, A.Wojtczak, M.Jaskolski, M.Gilski, J.G.Haasnoot, J.Reedijk:
  The crystal and molecular structures of dichlorobis(5,7-diphenyl-1,2,4-triazolo[1,5-a]pyrimidine)zinc(II) (1) and dichlorobis(5,7-diphenyl-1,2,4-triazolo[1, 5-a]pyrimidine)cobalt(II) (2).
  Inorg. Chim. Acta 260, 145-150 (1997).
• Sz.Krzywda, G.N.Murshudov, A.M.Brzozowski, M.Jaskolski, E.E.Scott, S.A.Klizas, Q.H.Gibson, J.Olson, A.J.Wilkinson (1998),
  Stabilizing Bound O2 in Myoglobin by Valine68 (E11) to Asparagine Substitution.
  Biochemistry 37, 15896-15907 (1998). [PubMed]

Hydrogen bond

• M.Jaskolski, M.Gdaniec, Z.Kosturkiewicz (1977),
  N-(N-Piperidylacetyl)piperidinium Perchlorate.
  Acta Cryst. B33, 1627-1630.
• M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz (1977),
  Quinoline-2-carboxamide.
  Acta Cryst. B33, 3558-3561.
• M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz (1977),
  Quinoline-2-carboxamide Hemihydrate.
  Acta Cryst. B33, 2284-2286.
• M.Jaskolski (1978),
  1-(Piperidinoacetyl)piperidine (PAcP).
  Acta Cryst. B34, 3429-3430.
• M.Jaskolski, M.Gdaniec, Z.Kosturkiewicz, M.Szafran (1978),
  Very Short Hydrogen Bond: X-Ray Structure of 2,6-Dimethylpyridine N-oxide Semiperchlorate.
  Pol. J. Chem. 52, 2399-2404.
• M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz (1979),
  Crystal and Molecular Structure of N-Phenyl-nicotinamide.
  Pol. J. Chem. 53, 2563-2569.
• M.Jaskolski, Z.Kosturkiewicz, D.Mickiewicz-Wichlacz, M.Wiewiorowski (1979),
  Synthesis and Crystal and Molecular Structure of 1,2-Di(N-piperidyl)ethane-bis-N-oxide Tetrahydrate.
  J. Mol. Struct. 52, 77-94.
• M.Gdaniec, M.Jaskolski, Z.Kosturkiewicz (1980),
  Crystal and Molecular Structure of 4-Methylquinoline-2-carboxamide. Pol. J. Chem. 54, 1539-1544.
• M.Jaskolski (1982),
  1,2-Di(N-piperidyl)ethane-bis-N-oxide Diperchlorate.
  Pol. J. Chem. 56, 187-193.
• M.Jaskolski, M.Gdaniec, Z.Kosturkiewicz:
  X-Ray Study on a System with Short O...O Intramolecular Hydrogen Bond. Crystal and Molecular Structure of 1, 2-Di(N-Piperidyl)ethane-bis-N-oxide Monoperchlorate.
  Pol. J. Chem. 56, 297-305 (1982).
• M.Jaskolski, I.Olovsson, R.Tellgren, D.Mickiewicz-Wichlacz:
  A Neutron Diffraction Study of 1,1'-Ethylenebis(piperidine 1-oxide) Monoperchlorate.
  Acta Cryst. B38, 291-294 (1982).
• M.Jaskolski, Z.Kosturkiewicz (1984),
  Structure of 1,2-Dipiperidiniethane Mono-N-oxide Monoperchlorate Monohydrate, (C12H25N2O)+.ClO4-.
  Acta Cryst. C40, 869-871.
• M.Plywaczyk, E.Tykarska, M.Jaskolski, Z.Kosturkiewicz (1984),
  Structure of 2-Benzoyl-1,2,3,4-Tetrahydro-1-isoquinolinecarbonitrile, C17H14N2O.
  Acta Cryst. C40, 1107-1109.
• A.Gzella, U.Rychlewska, M.Jaskolski, Z.Kosturkiewicz (1984), Acta Cryst. C40, 2098-2100.
• M.Jaskolski:
  Very Bent D-H...A Hydrogen Bonds: an Angular Criterion.
  Pol. J. Chem. 58, 955-957 (1984).
• E.Tykarska, M.Jaskolski, Z.Kosturkiewicz (1985),
  Structure of 2-Benzoyl-1,2-Dihydro-1-isoquinolinecarbonitrile.
  Acta Cryst. C41, 1792-1794.
• B.Urbaniak, M.Jaskolski, M.Rozwadowska, Z.Kosturkiewicz (1986),
  Structure of 2-(p-Toluenesulfonyl)-1,2,3,4-tetrahydroisoquinoline.
  Acta Cryst. C42, 1807-1809.
• E.Tykarska, M.Jaskolski, Z.Kosturkiewicz (1986),
  Structure of Ethyl-1-cyano-1,2-dihydro-2-isoquinolinecarboxylate.
  Acta Cryst. C42, 738-740.
• I.Olovsson, M.Jaskolski:
  Reaction Coordinate for the Proton Transfer in Some Hydrogen Bonds.
  Pol. J. Chem. 60, 759-766 (1986).
• J.Baran, Z.Dega-Szafran, M.Jask?lski, M.K.Marchewka, H.Ratajczak, M.Szafran:
  X-ray, phase transition, IR and Raman studies of the solid cpmplex of bis(pyridine betaine)-sulphuric acid.
  J.Mol.Struct. 406, 127-135 (1997).
• M.Szafran, M.Jaskolski, I.Kowalczyk, Z.Dega-Szafran:
  Structure, conformation and hydrogen bonding of some pyridiniumpropionate complexes.
  J. Mol. Struct. 448, 77-89 (1998).
• J.Wasicki, M.Jaskolski, Z.Pajak, M.Szafran, Z.Dega-Szafran, M.A.Adams, S.F.Parker:
  Crystal structure and molecular motion in pyridine N-oxide hemiperchlorate.
  J. Mol. Struct. 476, 81-95 (1999).
• Z.Dega-Szafran, M.Jaskolski, M.Szafran:
  OHO hydrogen bond and electrostatic interactions in a complex of pyridine betaine with phenylacetic acid studied by X-ray diffraction, FTIR spectroscopy and PM3, DFT calculations.
  J. Mol. Struct. 555, 191-200 (2000).
• E.Bartoszak-Adamska, G.Wojciechowski, M.Jaskolski, B.Brzezinski:
  Cooperative intramolecular hydrogen bonds in the structure of 5,5'-dibromo-3-diethylaminomethyl-2,2'-biphenol.
  J. Mol. Struct. 525, 253-259 (2000).
• Z.Dega-Szafran, M.Jaskolski, I.Kurzyca, P.Barczynski, M.Szafran (2001),
  Molecular structure, hydrogen bonding, basicity and spectroscopic properties of N,N'-dimethylpiperazine betaines and their hydrohalides.
  J. Mol. Struct. 614, 23-32.
• Z.Dega-Szafran, M.Jaskolski, M.Szafran, E.Dulewicz (2001),
  Bis(N-methylpiperidine betaine) hydrobromide: crystal structure and hydrogen bonding.
  J. Mol. Struct. 615, 33-43.
• Z.Dega-Szafran, M.Szafran, A.Addlagatta, M.Jaskolski (2001),
  Crystal structure and vibrational spectrum of bis(N-methyl-piperidine betaine) hexafluorosilicate.
  J. Mol. Struct. 598, 267-276.
• Z.Dega-Szafran, M.Jaskolski, I.Kurzyca, P.Barczynski, M.Szafran (2002),
  Molecular structure, hydrogen bonding, basicity and spectroscopic properties of N,N'-dimethylpiperazine betaines and their hydrohalides.
  J. Mol. Struct. 614, 23-32.
• Z.Dega-Szafran, M.Szafran, E.Dulewicz, A.Addlagatta, M.Jaskolski (2003),
  Crystal and molecular structure of N-methylpiperidine betaine hydrochloride.
  J. Mol. Struct. 654, 71-80.
• E.Bartoszak-Adamska, Z.Dega-Szafran, M.Przedwojska, M.Jaskolski (2003),
  Crystal and molecular structure of 1:1 complex of N-methylmorpholine betaine with salicylic acid.
  Pol. J. Chem. 77, 1711-1722.
• Z.Dega-Szafran, M.Szafran, E.Dulewicz, A.Addlagatta, M.Jaskolski (2004),
  Crystal and molecular structure of bis(N-methylpiperidine betaine) hydroiodide.
  J. Mol. Struct. 691, 217-225.
• M.Szafran, Z.Dega-Szafran, R.Thaimattam, M.Jaskolski (2004),
  Crystal and molecular structure of N-methylpiperidine betaine hydrofluoride.
  J. Mol. Struct. 706, 49-55.
• Z.Dega-Szafran, M.Szafran, M.Jaskolski, E.Dulewicz (2004),
  Effect of counter ion and stoichiometry on the structure, hydrogen bonding and conformation of N-methylpiperidine betaine hydrohalides.
  Ann. Soc. Chem. Pol. 3, 399-402.
• M.Szafran, B.Nowak-Wydra, M.Jaskolski, E.Bartoszak-Adamska, A.Szwajca, Z.Dega-Szafran (2005),
  Structures of pyrido[1,2a]pyrazinium and pyrido[1,2c][1,4]oxazonium bromides studied by 1H, 13C and 15N NMR, FTIR, X-ray and DFT methods.
  J. Mol. Struct. 743, 7-20.
• M.Szafran, Z.Dega-Szafran, M.Jaskolski, A.Addlagatta, E.Dulewicz (2005),
  The influence of halide anions on the molecular structure of bis(N-methylpiperidine betaine) monocation with short hydrogen bond.
  J. Mol. Struct. 741, 171-181.
• Z.Dega-Szafran, M.Jaskolski, M.Szafran (2006),
  Crystal and molecular structure of 1:1 complex between piperidine-3-carboxylic acid and p-hydroxybenzoic acid studied by X-ray diffraction, FTIR, 1H and 13C N MR spectroscopy, and DFT methods.
  Pol. J. Chem. 81, 931-946.
• Z.Dega-Szafran, E.Dulewicz, M.Szafran, R.Thaimattam, M.Jaskolski (2007),
  Structure, conformation and hydrogen bonding of 4-(N-methylpiperidinium)-butyric acid bromide.
  J. Mol. Struc. 828, 19-24.
• E.Bartoszak-Adamska, Z.Dega-Szafran, M.Krociak, M.Jaskolski, M.Szafran (2009),
  Hydrogen bonds in 1:1 complex of piperidine-3-carboxylic acid with salicylic acid.
  J. Mol. Struct. 920, 68-74.
• E.Bartoszak-Adamska, Z.Dega-Szafran, M.Jaskolski, M.Szafran (2009),
  Structural studies of a very short OHO hydrogen bond in bis(4-(N-methylpiperidinium)-butyrate) hydrobromide.
  J. Phys. Org. Chem. 22, 356-361.
• I.Kowalczyk, E.Bartoszak-Adamska, M.Jaskolski, Z.Dega-Szafran, M.Szafran (2010),
  Structure of 1-H-2-oxo-2,3-dihydroimidazo[1,2-a]pyridinium perchlorate by X-ray diffraction, DFT calculations and by FTIR and NMR spectroscopy.
  J. Mol. Struct. 976, 119-128.
• E.Bartoszak-Adamska, Z.Dega-Szafran, M.Jaskolski, M.Szafran (2011),
  Diastereomeric complex of (R/S)-piperidine-3-carboxylic acid with (2R,3R)-tartaric acid: Structural, spectroscopic and computational studies.
  J. Mol. Struct. 999, 98-105.

Proton sponges

• E.Bartoszak, M.Jaskolski, T.Gustaffson, .Olovsson, E.Grech:
  Structure of Thiocyanate Salt of 1, 8-bis(Dimethylamino)naphthalene (DMAN+SCN-) at 188 and 290 K.
  Acta Cryst. B50, 358-363 (1994).
• E.Bartoszak, Z.Dega-Szafran, M.Grundwald-Wyspianska, M.Jaskolski, M.Szafran:
  X-Ray, FT-IR, 1H and 13C NMR, and PM3 Studies of (N-H.N)+ and (O-H.O)- Intramolecular Hydrogen Bonds in a Complex of 1,8-Bis(dimethylamino)naphthalene with Maleic Acid.
  J. Chem. Soc. Faraday Trans. 2085-2094 (1993).
• E.Bartoszak, Z.Dega-Szafran, M.Jaskolski, M.Szafran:
  X-Ray, FT-IR, 1H and 13C NMR, PM3 and AM1 Studies of (N-H.N)+ and (O-H.O)- Hydrogen Bonds in a Complex of 1,8-Diaminonaphthalene with Maleic Acid: Proton Cavity and Basicity of Proton Sponges.
  J. Chem. Soc. Faraday Trans. 91, 87-92 (1995).
• E.Bartoszak-Adamska, E.Grech, M.Jaskolski:
  X-ray, IR and 1H NMR Studies of 1:1 Adduct of 1,8-Bis(dimethylamino)naphthalene (DMAN) and 1,1-Cyclobutanedicarboxylic Acid (CBDC).
  Pol. J. Chem. 72, 347-354 (1998).
• E.Bartoszak-Adamska, M.Jaskolski, B.Brzezinski:
  Crystal chemistry of protonated 1,2-bis(di-R-aminomethyl)benzenes. Part I: 1,2-bis(dimethylaminomethyl)benzene perchlorate.
  J. Mol. Struct. 446, 229-234 (1998).
• E.Bartoszak-Adamska, M.Jaskolski, B.Brzezinski:
  Crystal chemistry of protonated 1,2-bis(di-R-aminomethyl)benzenes. Part II: 1,2-bis(dimethylaminomethyl)benzene nitrate.
  J. Mol. Struct. 448, 57-62 (1998).
• E.Bartoszak-Adamska, M.Jaskolski, B.Brzezinski:
  Crystal chemistry of protonated 1,2-bis(di-R-aminomethyl)benzenes. Part III: 1,2-bis(diethylaminomethyl)benzene perchlorate.
  J. Mol. Struct. 475, 167-173 (1999).
• E.Bartoszak-Adamska, M.Jaskolski, H.Urjasz, B.Brzezinski (2005),
  Crystal chemistry of protonated 1,2-bis(di-R-aminomethyl)benzenes. Part VII: 1,2-bis(dipropylaminomethyl)benzene perchlorate.
  J. Mol. Struct. 738, 271-274.

Crystal engineering

• M.Gilski, M.Jaskolski:
  Molecular Recognition Motifs in Cytidinium and 2'-Deoxycytidinium Salts with Composite Anions.
  Acta Biochim. Polon. 45, 917-928 (1998). [PubMed]
• A.Anthony, M.Jaskolski, A.Nangia, G.R.Desiraju:
  Isostructurality in crystalline oxa-androgenes. A case of C-O-H...O and C-H...O interaction mimicry and solid solution formation.
  Chem. Commun. 1998, 2537-2538 (1998).
• A.Anthony, A.Nangia, M.Jaskolski:
  Crystal chemistry of some synthetic 2-oxa-steroids: conformation, packing motifs and isostructurality.
  Acta Cryst. B56, 512-525 (2000). [PubMed]
• P.Vishweshwar, R.Thaimattam, M.Jaskolski, G.R.Desiraju (2002),
  Supramolecular synthons based on N-H...N and C-H...O hydrogen bonds. Crystal engineering of a helical structure with 5,5-diethylbarbituric acid.
  Chem. Commun. 2002, 1830-1831. [PubMed]
• S.Aitipamula, P.K.Thallapally, R.Thaimattam, M.Jaskolski, G.R.Desiraju (2002),
  Topological Equivalences between Organic and Coordination Polymer Crystal Structures: An Organic Ladder formed with three-connected Molecular and Supramolecular Synthons.
  Org. Lett. 4, 921-924. [PubMed]
• S.Aitipamula, G.R.Desiraju, M.Jaskolski, A.Nangia, R.Thaimattam (2003),
  Multiple molecules in the crystallographic asymmetric unit. An alternative mode of close packing of networks of rigid hydrogen bonded molecules.
  Cryst. Eng. Commun. 5, 447-450.
• S.Aitipamula, A.Nangia, M.Jaskolski, R.Thaimattam (2003),
  Hydrogen bond networks in tris(4-hydroxyphenyl)methane and its 1:1 molecular complex with 4,4'-bipyridine.
  Acta Cryst. C59, o481-o484. [PubMed]
• B.K.Saha, A.Nangia, M.Jaskolski (2005),
  Crystal engineering with hydrogen bonds and halogen bonds.
  Cryst. Eng. Commun. 7, 355-358.
• R.Thaimattam, M.Szafran, Z.Dega-Szafran, M.Jaskolski (2008),
  Conformational richness and multiple Z' in salt co-crystal of N-methylpiperidine betaine with N-methylpiperidine betaine haxafluorosilicate.
  Acta Cryst. B64, 483-490. [PubMed]
• M.Wierzbicki, M.Gilski, K.Rissanen, M.Jaskolski, A.Szumna (2014),
  Experiences with application of macromolecular tools in supramolecular crystallography.
  Cryst. Eng. Commmun. 16, 3773-3780. [DOI]
• M.Szymanski, M.Wierzbicki, M.Gilski, H.Jedrzejewska, M.Sztylko, P.Cmoch, O.Shkurenko, M.Jaskolski, A.Szumna (2016),
  Mechanochemical Encapsulation of Fullerenes in Peptidic Containers Prepared by Dynamic Chiral Self-sorting and Self-assembly.
  Chemistry - A European Journal 22, 3148-3155. [PubMed]
• K.Eichstaedt, K.Szpotkowski, M.Grajda, M.Gilski, S.Wosicki, M.Jaskolski, A.Szumna (2019),
  Self-assembly and ordering of peptide-based cavitands in water and DMSO - the power of hydrophobic effects combined with neutral hydrogen bonds.
  Chem. Eur. J. 25, 3091-3097. [PDF]
• M.Gilski, P.Bernatowicz, A.Sakowicz, M.P.Szymanski, A.Zalewska, A.Szumna, M.Jaskolski (2020),
  C60 in a peptidic cage: a case of symmetry mismatch studied by crystallography and solid-state NMR.
  Acta Cryst. B76, 815-824. [DOI]

Methodology

• M.Jaskolski:
  A Comparison of Two Methods for the Calculation of Pseudorotation Parameters.
  Acta Cryst. A40, 364-366 (1984).
• M.Jaskolski, L.Lomozik:
  A Note on the Application of Significance Tests Based on the R-factor Ratio to the Selection of Species in Complex-formation Equilibria.
  Talanta 32, 511-512 (1985).
• M.Jaskolski:
  Is the Deformation Energy of a Molecular Fragment in Crystals Distributed According to a Boltzmann-like Law?
  Pol. J. Chem. 60, 263-267 (1986).
• L.Lomozik, M.Jaskolski, A.Wojciechowska:
  A Multistage Verification Procedure for the Selection of Models in the Studies of Complex Formation Equilibria.
  Pol. J. Chem. 65, 1797-1807 (1991).
• M.Jaskolski:
  A Note on the Structure Determinations of Putrescinium Monohydrogenphosphate Dihydrate.
  J. Solid State Chem. 487-489 (1992).
• Z.Dauter, M.Jaskolski:
  2'-Deoxycytidine Hemidihydrogenphosphate: Comparison of Crystal Structure Refinements Based on Diffractometer and Image Plate Data.
  Pol. J. Chem. 70, 1018-1029 (1996).
• M.Jaskolski, A.Wlodawer:
  A Minimalist's Approach to the Phase Problem - Phasing Selenomethionyl Protein Structures Using CuKa Data.
  Acta. Cryst. D52, 1075-1081 (1996).
• M.Cyranski, M.Gilski, M.Jaskolski, T.M.Krygowski (2003),
  On the Aromatic Character of the Heterocyclic Bases of DNA and RNA.
  J. Org Chem. 68, 8607-8613. [PubMed]
• M.Jaskolski, M.Li, G.Laco, A.Gustchina, A.Wlodawer (2006),
  Molecular replacement with pseudosymmetry and model dissimilarity: a case study.
  Acta Cryst. D62, 208-215. [PubMed]
• M.Jaskolski, M.Gilski, Z.Dauter, A.Wlodawer (2007),
  Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?
  Acta Cryst. D63, 611-620. [PubMed]
• M.Jaskolski, M.Gilski, Z.Dauter, A.Wlodawer (2007),
  Numerology versus reality: a voice in a recent dispute.
  Acta Cryst. D63, 1282-1283. [PubMed]
• O.Pasternak, A.Bujacz, J.Biesiadka, G. Bujacz, M.Sikorski, M.Jaskolski (2008),
  MAD phasing using the (Ta6Br12)2+ cluster: a retrospective study.
  Acta Cryst. D6464, 595-606. [PubMed]
• Z.Dauter, M.Jaskolski, A.Wlodawer (2010),
  Impact od synchrotron radiation on macromolecular crystallography: A personal view.
  J. Synchrotron Rad. 17, 433-444. [PubMed]
• J.Sliwiak, M.Jaskolski, Z.Dauter, A.McCoy, R.J.Read (2014),
  Likelihood-based molecular replacement solution for a highly pathological crystal with tetartohedral twinning and seven-fold translational non-crystallographic symmetry.
  Acta Cryst. D70, 471-480. [PDF]
• Z.Dauter, A.Wlodawer, W.Minor, M.Jaskolski, B.Rupp (2014),
  Avoidable errors in macromolecular structures - an impediment to efficient data mining.
  IUCrJ 1, 179-193. [OpenAccess]
• M.Kowiel, M.Jaskolski, Z.Dauter (2014),
  ACHESYM: an algorithm and server for standardized placement of macromolecular models in the unit cell.
  Acta Cryst. D70, 3920-3928. [PubMed]
• I.Shabalin, Z.Dauter, M.Jaskolski, W.Minor, A.Wlodawer (2015),
  Crystallography and chemistry should always go together: a cautionary tale of protein complexes with cisplatin and carboplatin.
  Acta Cryst. D71, 1965-1979. [PubMed]
• M.Malinska, M.Dauter, M.Kowiel, M.Jaskolski, Z.Dauter (2015),
  Protonation and geometry of histidine rings.
  Acta Cryst. D71, 1444-1454. [PubMed]
• M.Gilski, P.Drozdzal, R.Kierzek, M.Jaskolski (2016),
  Atomic-resolution structure of a chimeric DNA-RNA Z-type duplex in complex with Ba2+ ions: a case of complicated multi-domain twinning.
  Acta Cryst. D72, 211-223. [PubMed]
• M.Chwastyk, M.Jaskolski, M.Cieplak (2016),
  The volume of cavities in proteins and virus capsids.
  Proteins 84, 1275-1286. doi: 10.1002/prot.25076 [PubMed]
• M.Kowiel, D.Brzezinski, M.Jaskolski (2016),
  Conformation-dependent restraints for polynucleotides: I. clustering of the geometry of the phosphodiester group.
  Nucleic Acids Res. 44, 8479-8489. [OpenAccess]
• M.Kowiel, D.Brzezinski, P.J.Porebski, I.G.Shabalin, M.Jaskolski, W.Minor (2018),
  Automatic recognition of ligands in electron density by machine learning.
  Bioinformatics 35, 452-461. [PubMed]
• J.Raczynska, I.Shabalin, W.Minor, A.Wlodawer, M.Jaskolski (2018),
  A close look onto structural models and primary ligands of metallo-beta-lactamases.
  Drug Resistance Updates 40, 1-12. [DRU] or [PubMed]
• M.Gilski, J.Zhao, M.Kowiel, D.Brzezinski, D.H.Turner, M.Jaskolski (2019),
  Accurate geometrical restraints for Watson-Crick base pairs.
  Acta Cryst. B75, 235-245. [OpenAccess]
• M.Kowiel, D.Brzezinski, M.Gilski, M.Jaskolski (2020),
  Conformation-dependent restraints for polynucleotides: The sugar moiety.
  Nucleic Acids Res. 48, 962-973. [OpenAccess]
• D.Brzezinski, Z.Dauter, W.Minor, M.Jaskolski (2020),
  On the evolution of the quality of macromolecular models in the PDB.
  FEBS J. 287, 2685-2698. [PDF]
• A.Wlodawer, Z.Dauter, I.Shabalin, M. Gilski, D.Brzezinski, M.Kowiel, W.Minor, B.Rupp, M.Jaskolski (2020),
  Ligand-centered assessment of SARS-CoV-2 drug target models in the Protein Data Bank.
  FEBS J. 287, 3703-3718. [PDF]
• D.Brzezinski, M.Kowiel, D.R.Cooper, M.Cymborowski, M.Grabowski, A.Wlodawer, Z.Dauter, I.G.Shabalin, M.Gilski, B.Rupp, M.Jaskolski, W.Minor (2021),
  Covid-19.bioreproducibility.org: A web resource for SARS-CoV-2-related structural models.
  Protein Sci. 30, 115-124. [DOI]
• J.Smietanska, J.Sliwiak, M.Gilski, Z.Dauter, R.Strzalka, J.Wolny, M.Jaskolski (2020),
  A new modulated crystal structure of ANS complex of St Johns wort Hyp-1 protein with 36 protein molecules in the asymmetric unit of the supercell.
  Acta Cryst. D76, 653-667. [OpenAccess]
• M.Chwastyk, E.Panek, J.Malinowski, M.Jaskolski, M.Cieplak (2020),
  Properties of cavities in biological structures - a survey of the Protein Data Bank.
  Frontiers Molecular Biosciences 7, 591381. [OpenAccess]
• M.Jaskolski, Z.Dauter, I.Shabalin, M. Gilski, D.Brzezinski, M.Kowiel, B.Rupp, A.Wlodawer (2021),
  Crystallographic models of SARS-CoV-2 3CLpro: in-depth assessment of structure quality and validation.
  IUCrJ 8, 238-256. [OpenAccess]
• M.Grabowski, J.M.Macnar, M.Cymborowski, D.R.Cooper, I.G.Shabalin, M.Gilski, D.Brzezinski, M.Kowiel, Z.Dauter, B.Rupp, A.Wlodawer, W.Minor, M.Jaskolski (2021),
  Rapid Response to Emerging Biomedical Challenges and Threats.
  IUCrJ 8, 395-407. [OpenAccess]
• M.Jaskolski, A.Wlodawer, Z.Dauter, W.Minor, B.Rupp (2022),
  Group depositions to the Protein Data Bank need adequate presentation and different archiving protocol.
  Protein Sci. 31, 784-786. [DOI: https://doi.org/10.1002/pro.4271]

Education

• M.Jaskolski:
  Least-Squares Calculation of Pseudorotation Parameters in a Five-Membered Ring.
  J. Chem. Educ. 980-981 (1983).
• L.Lomozik, M.Jaskolski, A.Gasowska:
  Comparative Analysis of the Performance of the Computer Programs SCOGS, MINIQUAD, and SUPERQUAD in Studies of Complex-Formation Equilibria.
  J. Chem. Educ. 72, 27-30 (1995).
• M.Jaskolski:
  Integrating biocrystallography into traditional biology and chemistry curricula.
  J. Appl. Cryst. 34, 371-374 (2001).
• A.Wlodawer, W. Minor, Z.Dauter, M.Jaskolski (2008),
  Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures.
  FEBS J. 275, 1-21. [PDF]
• M.Jaskolski (2009),
  From atomic resolution to molecular giants: an overview of crystallographic studies of biological macromolecules with synchrotron radiation.
  Acta Phys. Polon. A 117, 257-263.
• Z.Dauter, M.Jaskolski (2010),
  How to read (and understand) Volume A of International Tables for Crystallography: an introduction for nonspecialists.
  J. Appl. Cryst. 43, 1150-1171. [DOI]
• M.Jaskolski (2010),
  Krystalografia dla biologow. Wydawnictwo Naukowe UAM Poznan.
• Z.Dauter, M.Jaskolski (2011),
  Zastosowanie promieniowania synchrotronowego w krystalografii bialek. In: Promieniowanie synchrotronowe w spektroskopii i badaniach strukturalnych. Wybrane zagadnienia (B.J.Kowalski, W.Paszkowicz, E.A.Gorlich, eds.), pp. 305-328. PTPS Krakow.
• A.Wlodawer, W.Minor, Z.Dauter, M.Jaskolski (2013),
  Protein crystallography for aspiring crystallographers, or how to avoid pitfalls and traps in macromolecular structure determination.
  FEBS J. 280, 5705-5736. [OpenAccess]
• M.Jaskolski, A.Wlodawer, Z.Dauter, I.Shabalin, M.Chruszcz (2021),
  Celebrating the 75th birthday of Professor Wladek Minor, one of the most accomplished Polish-American structural biologists.
  Acta Biochim. Polon. 68, 1-4. [PDF]
• W.Minor, M.Jaskolski, S.J.Martin, Z.Dauter (2021),
  Dr. Alexander Wlodawer - celebrating five decades of service to the structural biology community.
  FEBS J. 288, 4160-4164. [PDF]
• K.Dziubek, M.Jaskolski, A.B.Wieckowski (2023),
  O mitach w nauce na kanwie oryginalnej aparatury Lauego (Upon mythos in science: an example from the "original Laue apparatus").
  Nauka 1/2023, 107-121. DOI: 10.24425/nauka.2023.144949
• Z.Dauter, M.Jaskolski (2024),
  Zastosowanie promieniowania synchrotronowego w krystalografii białek.
  In: Promieniowanie synchrotronowe w fizyce i chemii ciała stałego: wybrane zagadnienia (B.J.Kowalski, W.Paszkowicz, E.A.Gorlich, eds.), pp. xxx-xxx. Wydawnictwo Naukowe UAM Poznan. DOI:

Curious

• M.Koralewski, M.Jaskolski (1983),
  Optical Properties of KHSO4 Single Crystal.
  Acta Phys. Polon. A63, 847-850.
• W.R.Dolbier, M.Gdaniec, E.Gomulka, M.Jaskolski, H.Koroniak:
  The Effect of Fluorine Substituents on the Structure of Cyclopropane. The Structure of 4,4,8,8-Tetrafluorotricyclo[5.1.0.0(3,5)]octane.
  Tetrahedron 40, 3945-3948 (1984).
• W.R.Dolbier, M.Gdaniec, M.Jaskolski, H.Koroniak:
  The Structure of syn-4,4,8,8-Tetrafluorotricyclo[5.1.0.0(3,5)]octane.
  J. Mol. Struct. 147, 155-160 (1986).
• Sz.Krzywda, M.Jaskolski, M.Gdaniec, Z.Dega-Szafran, M.Grundwald-Wyspianska, M.Szafran, Z.Dauter, G.Davies:
  Structure and FTIR spectra of 3:2 complexes of trimethylamine N-Oxide and 4-dimethylamine-2,6-dimethylpyridine N-oxide with perchloric acid.
  J. Mol. Struct. 375, 197-206 (1996).
• G.M.Zatorska, G.S.Dmytriv, V.V.Pavlyuk, E.Bartoszak-Adamska, M.Jaskolski (2002),
  Crystal structure of the new intermetallic compound Zr2-xLix+ySi1-y (x=0.17, y=0.12) and its relation with the disilicide ZrSi2.
  J. Alloys Comp. 346, 154-157.
• T.Stepkowski, K.Brzezinski, A.B.Legocki, M.Jaskolski, G.Bena (2005),
  Bayesian phylogenetic analysis reveals two-domain topology of S-adenosylhomocysteine hydrolase protein sequences.
  Mol. Phylogenet. Evol. 34, 15-28. [PubMed]
• A.Wlodawer, J.Lubkowski, W.Minor, M.Jaskolski (2010),
  Is too "creative" language acceptable in crystallography?
  Acta Cryst. D66, 1041-1042. [PDF]
• M.Jaskolski (2010),
  Personal remarks on the future of protein crystallography and structural biology.
  Acta Biochim. Polon. 57, 261-264. [PDF]
• E.Herrero, E.Kolmos, N.Bujdoso, Y.Yuan, M.Wang, M.C.Berns, H.Uhlworm, G.Coupland, R.Saini, M.Jaskolski, A.Webb, J.Gonalves, S.J.Davis (2012),
  EARLY FLOWERING4 Recruitment of EARLY FLOWERING3 in the Nucleus Sustains the Arabidopsis Circadian Clock.
  The Plant Cell 24, 428-443. [PDF]
• M.Jaskolski (2013),
  On the propagation of errors.
  Acta Cryst. D69, 1865-1866. [PubMed]
• M.Jaskolski (2014),
  Doing the right things.
  Acta Cryst. D70, 1. [PDF]
• M.Jaskolski, Z.Dauter, A.Wlodawer (2014),
  A brief history of macromolecular crystallography, illustarted by a family tree and its Nobel fruits.
  FEBS J. 281, 3985-4009. [PDF]
• Z.Dauter, M.Jaskolski (2014),
  Missed opportunities in crystallography.
  FEBS J. 281, 4010-4020. [PDF]
• M.Jaskolski, A.Wlodawer (2014),
  Celebrating the International Year of Crystallography.
  FEBS J. 281, 3983-3984. [PDF]
• J.Sliwiak, Z.Dauter, M.Kowiel, A.McCoy, R.J.Read, M.Jaskolski (2015),
  ANS complex of St Johns wort PR-10 protein with 28 copies in the asymmetric unit: a fiendish combination of pseudosymmetry with tetartohedral twinning.
  Acta Cryst. D71, 829-843. [OpenAccess]
• W.Minor, Z.Dauter, J.R.Helliwell, M.Jaskolski, A.Wlodawer (2016),
  Safeguarding structural databases against bad apples.
  Structure 24, 216-220. [PubMed]
• J.Raczynska, A.Wlodawer, M.Jaskolski (2016),
  Prior knowledge or freedom of interpretation? A critical look at a recently published classification of "novel" Zn binding sites.
  Proteins 84, 770-776. doi: 10.1002/prot.25024. [PubMed]
• M.Jaskolski, Z.Dauter (2016),
  Crystal pathologies in macromolecular crystallography.
  Postepy Biochemii 62, 401-407. [OpenAccess]
• W.Minor, Z.Dauter, M.Jaskolski (2016),
  The young person's guide to the PDB.
  Postepy Biochemii 62, 242-249. [OpenAccess]
• B.Rupp, A.Wlodawer, W.Minor, J.R.Helliwell, M.Jaskolski (2016),
  Correcting the record of structural publications requires joint effort of the community and journal editors.
  FEBS J. 283, 4452-4457. [OpenAccess]
• P.Drozdzal, M.Gilski, M.Jaskolski (2016),
  Ultrahigh-resolution centrosymmetric crystal structure of Z-DNA reveals the massive presence of alternate conformations.
  Acta Cryst. D72, 1203-1211. [PubMed]
• A.Wlodawer, Z.Dauter, P.Porebski, W.Minor, R.Stanfield, M.Jaskolski, E.Pozharski, C.X.Weichenberger, B.Rupp (2018),
  Detect, correct, retract: how to manage incorrect structural models.
  FEBS J. 285, 444-466. [OpenAccess]
• Z.Dauter, M.Jaskolski (2018),
  On the helical arrangements of protein molecules.
  Protein Sci. 27, 643-652. [PubMed]
• R.Saini, M.Jaskolski, S.Davis (2019),
  Circadian oscillator proteins across the kingdoms of life: structural aspects.
  BMC Biology 17, 13. [OpenAccess]
• P.Bierwagen, K.Szpotkowski, M.Jaskolski, A.Urbanowicz (2019),
  Borrelia Outer surface protein C is capable of human fibrinogen binding.
  FEBS J. 286, 2415-2428. [FEBS J]
• M.Grzechowiak, M.Ruszkowski, J.Sliwiak, K.Szpotkowski, M.Sikorski, M.Jaskolski (2019),
  Crystal structures of plant inorganic pyrophosphatase, an enzyme with a moonlighting autoproteolytic activity.
  Biochem. J. 476, 2297-2319. [PubMed]
• J.E.Raczynska, B.Imiolczyk, M.Komorowska, J.Sliwiak, J.Czyrko-Horczak, K.Brzezinski, M.Jaskolski (2020),
  Flexible loops of New Delhi metallo-beta-lactamase modulate its activity towards different substrates.
  Int. J. Biol. Macromol. 158, 104-115. [DOI]
• Z.Dauter, M.Jaskolski (2020),
  Multiplicity-weighted Euler's formula for symmetrically arranged space-filling polyhedra.
  Acta Cryst. A76, 580-583. [OpenAccess] DOI: 10.1107/S2053273320007093
• A.Pyrih, M.Jaskolski, A.K.Gzella, R.Lesyk (2021),
  Synthesis, structure and evaluation of anticancer activity of 4-amino-1,3-thiazolinone/pyrazoline hybrids.
  J. Mol. Struct. 1224, 129059. [DOI]
• P.Bierwagen, J.Sliwiak, M.Jaskolski, A.Urbanowicz (2021),
  Strong interactions between Salp15 homologues from the tick I. ricinus and distinct types of the outer surface OspC protein from Borrelia.
  Ticks and Tick-Born Diseases 12, 101630. [DOI]
• B.Naskrecki, Z.Dauter, M.Jaskolski (2021),
  Arithmetic proof of the multiplicity-weighted Euler's characteristic for symmetrically arranged space-filling polyhedra.
  Acta Cryst. A77, 126-129. [OpenAccess] DOI: 10.1107/S2053273320016186
• J-J.Liu, H.Fernandes, A.Zamany, M.Sikorski, M.Jaskolski, R.A.Sniezko (2021),
  In-vitro anti-fungal assay and association analysis reveal a role for the Pinus monticola PR10 gene (PmPR10-3.1) in quantitative disease resistance to white pine blister rust.
  Genome 64, 693-704. [PDF]
• M.Grzechowiak, B.Sekula, Z.Dauter, M.Jaskolski, M.Ruszkowski (2021),
  Serendipitous crystallization of E. coli HPII catalase, a sequel to the tale usually not told.
  Acta Biochim. Polon. 68, 29-31. [PDF]
• M.Ignasiak, K.Nowicka-Bauer, M.Grzechowiak, M.Sikorski, B.Shashikadze, M.Jaskolski, B.Marciniak (2021),
  Sensitized photo-oxidation of plant cytokinin-specific binding protein - Does the environment of the thioether group influence the oxidation reaction? From primary intermediates to stable products.
  Free Radical Biology and Medicine 165, 411-420. [PDF]
• B.Naskrecki, Z.Dauter, M.Jaskolski (2021),
  A topological proof of the modified Euler characteristic based on the orbifold concept.
  Acta Cryst. A77, 317-326. [OpenAccess] DOI: 10.1107/S2053273321004320
• B.Naskrecki, M.Jaskolski, Z.Dauter (2022),
  The Euler characteristic as a basis for teaching topology concepts to crystallographers.
  J. Appl. Cryst. 55, 154-167. [OpenAccess] DOI: 10.1107/S160057672101205X
• A.Pyrih, A.Lapinski, S.Zieba, R.Lesyk, M.Jaskolski, A.K.Gzella (2023),
  Proton tautomerism and stereoisomerism of 4-amino-1,3-thiazol-2(5H)-one derivatives bearing substituents with opposite electronic effects: synthesis, structure and spectroscopic studies.
  J. Mol. Struct. 1247, 134441. DOI: 10.1016/j.molstruc.2022.134441
• P.Drozdzal, T.Manszewski, M.Gilski,K.Brzezinski, M.Jaskolski (2023),
  Right-handed Z-DNA at ultrahigh resolution: a tale of two hands and the power of the crystallographic method.
  Acta Cryst. D79, 133-139. DOI: 10.1107/S2059798322011937
• K.Nowicka-Bauer, M.Grzechowiak, M.Ignasiak-Kciuk, T.Ravensborg, K.Frckowiak, O.Nrregaard Jensen, M.Jaskolski, B.Marciniak (2023),
  Does the presence of ground state complex between a PR-10 protein and a sensitizer affect the mechanism of sensitized photo-oxidation?
  Free Radical Biology and Medicine 198, 27-43. DOI: 10.1016/j.freeradbiomed.2023.01.022
• A.Pyrih, A.Lapinski, S.Zieba, R.Lesyk, M.Jaskolski, A.K.Gzella (2023),
  Proton tautomerism in 5-ylidene-4-(o-, m-, p-hydroxyphenyl)amino-1,3-thiazol-2(5H)-one derivatives: synthesis, crystal structure, and spectroscopic studies.
  Acta Cryst. B79, 220-232. DOI: 10.1107/S2052520623003852
• A.Pyrih, A.Lapiński, S.Zieba, A.Mizera, R.Lesyk, A.K.Gzella, M.Jaskolski (2023),
  Proton tautomerism and stereoisomerism in 5-dimethylaminomethylidene-4-(m-, p-trifluoromethylphenyl)amino-1,3-thiazol-2(5H)-ones: crystal structure and spectroscopic studies.
  Acta Cryst. C79, 480-490. DOI: 10.1107/S2053229623009087
• A.Pyrih, A.Lapiński, S.Zieba, A.Mizera, R.Lesyk, A.Gzella, M.Jaskolski (2024),
  Proton tautomerism and stereoisomerism in isomeric 4-(metoxyphenyl)amino-1,3-thiazol-2(5H)-one derivatives: synthesis, crystal structure and spectroscopic studies.
  J. Mol. Struct. 1295, 136748. DOI: 10.1016/j.molstruc.2023.136748
• M.Jaskólski (2023),
  Biologia strukturalna: historia, teraźniejszość, perspektywy.
  Nauka 4/2023, 17-36. DOI: 10.24425/nauka.2023.148224
• M.Jaskólski (2024),
  Biologia strukturalna wczoraj, dziś, jutro ?
  W: Uniwersytet - otwarte przestrzenie dyskursów (red. I.Cytlak, K.Przyszczypkowski), pp. 213-224. Wydawnictwo Naukowe UAM, Poznań. DOI: 10.14746/amup.9788323242703

Last update: July 4, 2024