Research at CBB
X-Ray crystallography has been and
continues to be the major source of information about the three-dimensional
structure of macromolecules. Typically, crystallographic studies of the
structure of a macromolecule are divided into several steps. First, the
biomolecule under study has to be obtained in crystalline form, often a
success-limiting step. Next, the crystals are exposed to X-rays and the
diffraction pattern is recorded. The diffraction pattern is then the basis
for the structure determination process. The Center is equipped and prepared
to carry out all the steps necessary for macromolecular structure determination,
from protein purification and crystallization, through low-temperature
diffraction experiments, to structure evaluation and analysis. The biomolecules
studied in the Center include both proteins and nucleic acids.
research activities and major results
3D Domain swapping and amyloidogenesis
Amyloid-forming proteins attract attention because of their role in the pathogenesis of a number
of diseases, like Alzheimer's disease and the prionoses. The pathophysiological processes involve abnormal conformational
changes, followed by aggregation. Human cystatin C (HCC), a potent and abundant inhibitor of cysteine proteases, changes its
structure on prolonged incubation to form inactive dimers. The tendency to oligomerize may explain why HCC forms amyloid
deposits in the brain arteries at advanced age. Formation of HCC amyloid is accompanied by the presence of HCC dimers in the
cerebrospinal fluid. The amyloidogenic property of HCC is drastically amplified in the endemically occurring L68Q mutant that
causes amyloidosis and brain hemorrhage leading to death in young adults. We have reported, for the first time, the crystal
structure of HCC and demonstrated that the protein aggregates to form dimers through an exchange of structural units. This
phenomenon of 3D domain swapping is a mechanism for oligomerization of monomeric proteins. The same
mechanism of 3D
domain swapping has been found for N-truncated HCC, which is the dominating material isolated from cystatin C deposits of
patients suffering from HCC amyloidosis. The structure of 3D domain-swapped HCC dimers suggests possible mechanisms of amyloid
fibril formation and explains the role of the L68Q mutation. It also has implications for other diseases involving
conformational pathologies. In recent experiments, we have demonstrated that by strategic placement of cysteine residues in the
HCC sequence, we can introduce new disulfide bridges, allowing red-ox control of domain swapping, and in consequence - control
of dimerization, oligomerization, and amyloid fibril formation.
Cysteine proteases and their inhibitors
Several serious diseases related to tissue degeneration, such as osteoporosis or muscular
dystrophy, are linked to abnormalities in the functioning of cysteine proteases. There is a variety of natural inhibitors of
these enzymes, ranging from sizeable proteins, such as cystatins, to relatively small molecules, such as E-64. The latter
compound contains an oxirane ring that blocks the enzyme by forming a covalent bond with the catalytic thiol group. We have
studied a number of complexes of the model cysteine protease papain with synthetic inhibitors containing a peptide sequence
modeled after the binding epitope of HCC, and a reactive group, such as oxirane or diazomethylketone. Cysteine proteases are
also involved in pathogen invasion. We have determined the crystal structure of the wild-type zymogen (known as superantigen B)
of the enzyme from the highly virulent bacterium Streptococcus pyogenes. In another project, we focus on the cysteine
protease inhibitor, called chagasin, from the protozoan responsible for Chagas disease, Trypanosoma cruzi. Although chagasin has
the same size as cystatins, our crystal structure has demonstrated that it has a completely unrelated fold. Nevertheless, the
enzyme-binding epitope has the same three-loop architecture, as revealed by the crystal structures of inhibitory complexes
between chagasin and the human enzymes cathepsin L and B and the model cysteine protease papain.
Retroviral protease is a key enzyme in the replication cycle of the HIV-1 retrovirus, the
causative agent of AIDS. Since the determination of the three-dimensional structure of the enzyme (in a collaborative project with Dr. Alex Wlodawer, NCI, USA) and the discovery that it is
a symmetric, homodimeric aspartic protease, it has become the main target in the rational design of drugs for the treatment of
AIDS. Our current interest in this field focuses on new-generation active-site inhibitors of HIV-1 protease as potential drugs, on complexes
of the enzyme with autodigestion products, and on proteases from other retroviruses. The recently determined structure of the enzyme from the leukemia-causing HTLV virus has revealed important
differences in the active-site architecture between the HIV-1 and HTLV enzymes, thus explaining the failure of successful
anti-AIDS drugs in the treatment of HTLV infections. Another retrovirus of interest is Mason-Pfizer Monkey Virus (M-PMV), which causes AIDS-like syndrome in rhesus monkeys.
M-PMV protease can be purified and crystallized as a monomer, and its structure (B; compare it with that of HIV-1 protease protomer extracted from the dimeric context, A)
is an important target for the design of dimerization inhibitors that could
be developed as a new-generation antiretroviral drugs. The structure of M-PMV protease has been solved in an unprecedented manner, using -- as a molecular-replacement
probe -- a model generated in a "citizen-science" experiment by players of the Foldit online game. We have also been studying the
structure of retroviral integrase, which
is responsible for the integration of the retroviral genetic material into the host cell genome. In particular, we have determined, again in a collaborative project with Dr. Alex Wlodawer,
the structure of the catalytic domain in active conformation and in complex with divalent metal cations.
Antileukemic bacterial asparaginases
The interest in periplasmic bacterial L-asparaginases
has been instigated by their antileukemic activity. Asparaginases of this
type, for example Escherichia coli L-asparaginase II (EcAII), are
homotetramers with four active sites. Each active site is created by amino
acids from two monomers, including amino acids form conserved motifs. The
mechanism of the asparaginase reaction is not fully understood. It could
be a variant of the reaction catalyzed by serine proteases, but with a
threonine in the role of the nucleophilic serine. The other residues of
the putative catalytic triad could be D90 and K162. To view an electronic
poster on the dynamics aspects of the L-asparaginase catalytic center click
here . The antitumor activity of these enzymes is the effect of their
high affinity for the substrate. Depletion of L-asparagine in the circulating
pools starves the tumor cells, which have reduced levels of L-asparagine
synthesis. We have studied a number of EcAII mutants to shed more light
on the enzymatic mechanism of these enzymes. Recently, we have discovered
that EcAII binds zinc cations, which may be of importance in its role as
In plants, L-asparagine is the most abundant metabolite for the storage and transport of
nitrogen that is utilized in protein biosynthesis. Asparagine hydrolysis in plants is catalyzed by asparaginases with no
homology to the bacterial-type enzymes. The most studied enzymes in this class, from legume plants, are involved in metabolic
pathways connected with assimilation of atmospheric nitrogen. We have cloned, sequenced, expressed, and crystallized the enzyme
from Lupinus luteus (LlA). We have also shown that the E. coli genome encodes a highly homologous enzyme, EcAIII.
of EcAIII has been solved demonstrating that it is an N-terminal nucleophile (Ntn) hydrolase that undergoes autoproteolytic
activation to liberate the N-terminal threonine (subunit beta) nucleophile. The active protein is an (alpha-beta)2
The structure and maturation pattern place EcAIII in one class with aspartylglucosaminidases. However, enzymatic and kinetic
studies show that both LlA and EcAIII are predominantly active as isoaspartyl aminopeptidases, and that their L-asparaginase
activity is of secondary importance. In this light, LlA and EcAIII gain in relevance as enzymes responsible for the degradation
of malformed proteins, in which a peptide bond occurs at the side chain of asparagine or aspartic acid.
Proteins involved in plant-bacterium symbiosis
Symbiosis between legume plants and nitrogen-fixing bacteria depends on exchange of precise
molecular signals. This process results in the formation of root nodules in which the bacteria assimilate atmospheric nitrogen.
In addition to plant signals, bacterial signals, called Nod Factors (NF), are also necessary. The unique NF biosynthetic pathway
includes about a dozen enzymes whose structure is very poorly understood. We have cloned,
overexpressed, and crystallized (also in selenomethionyl form) two rhizobial enzymes form this pathway (NodZ and NodS) and
determined their structure by the MAD method. NodZ catalyzes fucosylation of the NF chitooligosaccharide (COS) molecule. The
crystal structure reveals a two-domain folding pattern, with one of the domains folded according
to Rossmann motif. This is consistent with the fact that GDP-fucose is the sugar donor in the fucosylation reaction. NodS
N-methylates the non-reducing unit of the COS substrate, using SAM (S-adenosyl-L-methionine) as methyl donor. Our structures show
that the N-terminal part of the enzyme gets ordered on SAM binding, creating at the same time a deep canyon for COS docking. The
two substrates meet at an orifice leading to the SAM-cavity, where the NH2 nucleophile of COS attacks the CH3 group of SAM in the
Plant pathogenesis-related and hormone-binding proteins
The pathogenesis-related class 10 (PR-10) proteins have been detected in nearly all studied
plants but never in non-plant organisms. The PR-10 class includes numerous homologs with expression patterns responding to
pathogens and other stress factors. Tree pollen allergens are also in this class, similarly to the distantly related
cytokinin-specific binding proteins (CSBP). In contrast to CSBP, the function of classic PR-10 proteins remains unknown
despite their high cytosolic content. We have determined the crystal structure of a CSBP protein in complex with the plant
hormone zeatin, confirming that its fold is consistent with PR-10 classification. This fold consists of a seven-stranded
antiparallel beta-sheet wrapped around a long C-terminal helix. Between the sheet and the helix there is a large internal
cavity, where the ligands are bound. The C-terminal helix is unusual since it shows high sequence variability and geometrical
distortions. These distortions determine the shape and size of the cavity and may, therefore, control the ligand specificity of
the protein. Recently, we also managed to crystallize a classic PR-10 protein in complex with zeatin. In both complexes there
are multiple copies of the hormone in the binding cavity (CSBP - two, PR-10 - three) but the modes of binding are
On the other hand, the St John's wort protein Hyp-1, purportedly responsible for the biosynthesis of the
pharmacologically active hypericin, seems to be just a PR-10 protein, but it has an unusal pattern of three binding sites, illustrated here by a complex with the fluorescent dye ANS
(8-anilino-1-naphthalene sulfonate). In another study, we have shown that Nodulin 13 from Medicago truncatula (MtN13, involved in root nodulation during symbiosis with
nitrogen-fixing bacteria) is a PR-10 protein binding, upon its dimerization, different cytokinins in a very specific way, with 2:2 stoichiometry.
Insect hormone-binding proteins
The complicated insect development program is orchestrated by hormones, such as Juvenile Hormone
(JH). This very labile and highly hydrophobic molecule is transported in the insect hemolymph by a specialized protein called
Juvenile Hormone Binding Protein (JHBP), as a 1:1 complex. Recently, we solved the structure of this mysterious protein from
revealing its hot-dog-like fold, in which a long alpha-helix is almost completely wrapped in a highly curved beta-sheet. The
folding motif can be found in two low-homology human proteins, which also bind hydrophobic ligands, but it is present there in
tandem repeats, indicate gene duplication. Surprisingly, the relatively small JHBP protein contains two hydrophobic pockets,
one at each pole. Analysis of the interior of those pockets together with other biochemical experiments leaves no doubt as to
which of them harbors the hormone binding site. So far, it was not possible to obtain crystalline JHBP-JH complex. Every time
we try to soak the hydrophobic JH molecule into the JHBP crystals - they crack, hinting that there is a significant
conformational rearrangement of the protein molecule on hormone binding.
The functional nuclear receptor for the steroid hormones responsible for molting and
metamorphosis in insects is an unusual heterodimeric molecule. The crystal structure of the DNA-binding Domains (DBDs) of the
two partners (EcR and Usp) in complex with their natural DNA response element, hsp27, reveals a novel element (an alpha-helix)
in the C-Terminal Extension (CTE) of the EcRDBD domain. The location of this helix in the minor groove of the DNA target does not
match any of the locations reported previously for nuclear receptors. Mutational analyses suggest that this alpha-helix is a
component of an EcR-box, a novel element indispensable for DNA-binding.
RbcX is a chaperone assisting in the assembly of RuBisCO, the CO2 fixing complex that is the most
abundant protein on Earth. The dimeric RbcX protein has a boomerang shape with alpha-helix bundles on both ends and a pair of very
long helices reaching from one bundle to the other. The long helices have a very strong kink in the middle, which - according to
normal-mode analysis - is a hinge for a large-amplitude butterfly motion of the molecule. It is very likely that this "breathing"
motion of the RbcX molecule is connected with binding and release of the RuBisCO large subunit (RbcL) during RuBisCO assembly. c6
is a special cytochrome found in algae, cyanobacteria and plants where it acts in electron transfer between cytochrome b6f and
photosystem I (PSI). c6 has a covalently bound heme residue and is characterized by a very high redox potential of nearly 0.4 V.
We have determined atomic-resolution structures of c6 from a mesophilic cyanobacterium (Synechococcus) in the reduced and
Macromolecular structure at ultrahigh resolution
The crystal structure of a mutant of BPTI
(Bovine Pancreatic Trypsin Inhibitor) has been refined using low-temperature
synchrotron data extending to 0.86-A resolution to an R-factor of 0.1035.
From full-matrix least-squares refinement the accuracy of C-C bond distances
is 0.010 A. Many H-atoms could be seen in difference electron density maps,
including those in water molecules. The structure reveals a double-conformation
C14-C38 disulfide bridge and a salt bridge between the N- and C-termini.
It also provides examples of asparagine residues in unusual conformations
and illustrates the importance of N-H...pi hydrogen bonds in stabilizing
the molecular structure. As a result of the high resolution and high quality
of the electron-density maps, about 20% of all residues are found, and
successfully modeled, in alternate conformations. At this resolution the
refinement is highly overdetermined allowing for removal of main-chain
restraints and for unbiased verification of the stereochemical standards
used in protein structure refinements at lower resolution. This reveals,
for instance, that deviations up to 20 degrees from peptide bond planarity
are quite possible. Our crystal structure of Z-DNA refined at 0.53 A resolution
to R=0.067 without restraints, shows unusual regularity of the left-handed DNA
duplex in the absence of metal cations and indicates the need to revise some of the stereochemical standards
used in nucleic acid refinement at lower resolution.
The crystal structure of a Z-DNA hexamer has been solved from the anomalous signal of the P
atoms at copper wavelength. The multiplicity of the diffraction data was the most crucial single factor for the solution of the
phase problem. The structure was refined to an R factor of 0.089 at 0.95 A resolution. In another study, we have demonstrated
the power of the (Ta6Br12)2+ complex for phasing protein structures and determined the precise geometry and molecular
interactions of this cation in a protein crystal context. The crystals of Hyp-1 in complex with ANS turned out to have commensurately modulated superstructure with 28 protein molecules in
the asymmetric unit. The structure of this crystal (which also showed tetartohedral twinning) was solved (in collaboration with Prof. Randy Read, Univ. of Cambridge) by Molecular
Replacement despite extremely complex, seven-fold, translational Non-Crystallographic Symmetry (tNCS). Modulated crystal structures are extremely rare in macromolecular crystallography. We are
also developing Internet tools for teaching crystallography, available at this link (including a
PXQuiz) and here.
Our interest in this area is on hydrogen bonds as determinants of supramolecular organization,
with focus on both extremely strong (i.e. short) and very weak hydrogen bonds. In the latter category, we are interested in
C-H...X and Y-H...pi interactions. We have discovered interaction mimicry utilizing C-H...O bonds and leading to
one-dimensional isostructurality. Also, we have used the N-H...N and C-H...O synthons to engineer a supramolecular helix. When
applied to nucleoside salts, the concept of supramolecular synthons has revealed pre-ferred interaction patterns, also
including C-H donors. Our current focus is on co-crystals as potential vehicles for Active Pharmaceutical Ingredients (APIs).
Macromolecular Crystal Structures Solved Here
Cyanobacterial cytochrome c6
Bacterial L-asparaginase II
(pseudo enantiomorphic crystal pair of Y25F mutant of E. coli L-asparaginase and
Erwinia chrysanthemi L-asparaginase)
E. coli isoaspartyl aminopeptidase/L-asparaginase
Plant (left) and bacterial (right) isoaspartyl
aminopeptidase/L-asparaginase with surface potential and active site
Papain from Carica papaya
BPTI mutant: dual-conformation disulfide,water
molecules (PDBSummary for low-temperature
structure at 0.86 A)
CMTI (trypsin inhibitor from squash) mutant.
Four molecules of the protein coordinate a zinc cation
Glu side chains ( Zoom )
Class-10 Pathogenesis-Related protein from yellow
Cytokinin-specific binding protein (CSBP) from mung bean stores two
zeatin molecules in its binding
cavity, also shown in their 1.2 A electron density. See also the
(Ta6Br12)2+ cluster in its 1.8 A anomalous difference map at 15
sigma, which was used to solve the structure by MAD. * PDB:
Medicago truncatula nodulin MtN13 forms unusual dimers that bind cytokinin hormones (spheres) in a highly specific manner, by sealing the binding cavity
with a plug (blue) from the other binding partner.
Hyp-1, a PR-10 protein from St John's wort (Hypericum perforatum) in complex with ANS (8-anilino-1-sulfonate) forms monoclinic crystals that are tetartohedrally twinned and have
commensurately modulated superstructure, with seven-fold translational Non-Crystallographic Symmetry (tNCS) along the c direction. The asymmetric unit of this modulated crystal contains
28 protein molecules and 89 ANS ligands, occupying with variable frequency the three binding sites identified in the
NodZ - fucosyltransferase from Bradyrhizobium, involved in the
biosynthetic pathway of Nod
factor, through which
nitrogen-fixing soil bacteria signal their legume plant partners that they are ready to invade their
root hairs to establish symbiosis, which will allow the plant to assimilate atmospheric nitrogen. *
NodS N-methyltransferasefrom Bradyrhizobium methylates the Nod factor. The methyl
donor is SAM. After the reaction, SAM is converted to SAH, visible in the active site of the enzyme in this complex. On SAM
binding, the N-terminal part of the enzyme gets ordered creating a clear docking canyon for the
methyl-acceptor (COS) molecule.
S-adenosylhomocysteine (SAH) is a by-product, and strong inhibitor, of all cellular methylation
reactions that depend on S-adenosylmethionine (SAM). Therefore, fast removal (by
SAH hydrolase, or
SAHase) of SAH is necessary to keep the cell going. The structure of the enzyme from Lupinus
luteus is the first experimental model of a plant SAHase.
Juvenile Hormone Binding Protein (JHBP) from Galleria mellonella
binds the insect Juvenile Hormone (JH) that regulates metamorphosis and maturation. * PDB:
The heterodimeric ecdysteroid nuclear receptor DNA Dinding Domains (DBDs) of
EcR and Usp from Drosophila melanogaster in complex with their natural 20 bp hsp27 DNA
response element. * PDB:
Z-DNA structure refined at 0.53 A resolution in the absence of metal cations
3D Domain-swapped human cystatin C,
PDBSummary), also with beta-sheet aggregation
The protozoan Trypanosoma cruzi, the pathogen causing Chagas disease, expresses a potent
inhibitor of cysteine proteases called chagasin. The structure of a
complex between chagasin and the human cysteine protease cathepsin
L shows how the inhibitor (gold) cripples the enzyme (blue) by blocking its
active-site cleft with an epitope consisting of three loops. * PDB:
Met mioglobin V68N mutant
The RuBisCO chaperone protein RbcX
Structure of monomeric M-PMV retroviral protease (B), solved with a Foldit-generated model,
compared in electrostatic potential surface representation to a protomer of HIV-1 protease (A)
3D domain swapping
antileukemic bacterial asparaginases
plant pathogenesis-related proteins
high resolution protein crystallography
M.Chwastyk, M.Jaskolski, M.Cieplak (2016) The volume of cavities in proteins and virus capsids.
Proteins 84, 1275-1286.
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.
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.
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.
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, 1-10.
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.
W.Minor, Z.Dauter, J.R.Helliwell, M.Jaskolski, A.Wlodawer (2016) Safeguarding structural data repositories against bad apples.
Structure 24, 216-220.
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.
.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.
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.
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.
M.Malinska, M.Dauter, M.Kowiel, M.Jaskolski, Z.Dauter (2015) Protonation and geometry of histidine rings.
Acta Cryst. D71, 1444-1454.
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.
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.
Z.Dauter, M.Jaskolski (2014) Missed opportunities in crystallography.
FEBS J. 281, 4010-4020.
M.Jaskolski, Z.Dauter, A.Wlodawer (2014) A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits.
FEBS J. 281, 3985-4009.
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, 3290-3298.
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.
M.Wierzbicki, M.Gilski, K.Rissanen, M.Jaskolski, A.Szumna (2014) Experiences with applications of macromolecular tools in supramolecular crystallography.
CrystEngCom 16, 3773-3780.
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.
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.
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.
M.Ruszkowski, K.Szpotkowski, M.Sikorski, M.Jaskolski (2013) The landscape of cytokinin binding by a plant nodulin.
Acta Cryst. D69, 2365-2380.
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.
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.
H.Fernandes, K.Michalska, M.Sikorski, M.Jaskolski (2013) Structural and functional aspects of PR-10 proteins.
FEBS J. 280, 1169-1199.
A.Wojtkowiak, K.Witek, J.Hennig, M.Jaskolski (2013) Crystal structures of active-site mutant of plant 1,3--glucanase in complex with oligosaccharide products of hydrolysis.
Acta Cryst. D69, 52-62.
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.
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.
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.
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.
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.
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.
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.
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.
M.Jaskolski (2011) A new piece in the 3D jigsaw of malaria parasite. Structure 19, 901-902.
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 a retroviral protease folded as a
monomer. Acta Cryst. D67, 907-914.
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.
M.Orlikowska, E.Jankowska, R.Kolodziejczyk, M.Jaskolski, A.Szymanska (2011) Hinge-loop mutation can be used to control 3D domain swapping and amyloidogenesis of human cystatin C.
J. Struct. Biol. 173, 406-413.
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.
A.Wlodawer, J.Lubkowski, W.Minor, M.Jaskolski (2010) Is too "creative" language acceptable in crystallography? Acta Cryst.
Z.Dauter, M.Jaskolski, A.Wlodawer (2010) Impact od synchrotron radiation on macromolecular crystallography: A personal view. J.
Synchrotron Rad. 17, 433-444.
Z.Dauter, M.Jaskolski (2010) How to read (and understand) vol. A of International Tables for Crystallography: An introduction
for non-specialists. J. Appl. Cryst. 43, 1150-1171.
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.
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.
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.
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.
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.
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, 2926-2946.
K.Michalska, A.Hernandez-Santoyo, M.Jaskolski (2008) The mechanism of autocatalytic activation of plant-type L-asparaginases.
J. Biol. Chem. 283, 13388-13397.
I.Redzynia, A.Ljunggren, M.Abrahamson, J.S.Mort, J.C.Krupa, M.Jaskolski, G.Bujacz (2008) Structural basis of the successful
inhibition of human cathepsin B by a parasite inhibitor - chaginas. J. Biol. Chem. 283, 22815-22825.
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. D64, 595-606.
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.
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.
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.
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.
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.
Dr. Iva Pichova, Czech Academy of Sciences, Prague
Dr. David Baker, University of Washington, Seattle, WA, USA
Dr. Zbigniew Dauter, ANL/NCI, Argonne, IL, USA
Prof. Anders Grubb, Lund University, Sweden
amyloid structure, 3D domain swapping
Dr. Magnus Abrahamson, Lund University, Sweden
inhibitors of cysteine proteases
Prof. Jacek Otlewski, Wroclaw University
Prof. Andrzej Szczepaniak, Wroclaw University
Prof. Andrzej Dzugaj, Wroclaw University
Dr. Clare Sansom, Birkbeck College, London, UK
Prof. Randy Read, University of Cambridge, UK
Dr. Alexander Wlodawer, NCI-FCRDC, Frederick, MD, USA
Prof. Wladek Minor, University of Virginia, Charlottesville, VA, USA
Prof. Agnieszka Szumna, IChO PAN, Warsaw
Dr. Bernhard Rupp, CVMO, k.-k.Hofkristallamt, Vista, CA, USA
crystallographic methodology/quality control
National Science Centre SYMFONIA grant for
Supramolecular Peptide Organic Frameworks (POFs)
National Science Centre OPUS grant for
Structural studies of proteins crucial for tick-mammal-pathogen interactions
National Science Centre HARMONIA grant for
Exploiting the potential of synchrotron radiation for high resolution and weak signal in macromolecular crystallography
- DesInMBL Structure-guided design of pan inhibitors of metallo-beta-lactamases Project supported by the National Center for Research and Development (NCBR) within the
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Last update: March 27, 2017 (MJ)