Biological Crystallography

 

Acta Cryst. (2002). D58, 381-391  [ doi:10.1107/S0907444901021175 ]

The structure of the FERM domain of merlin, the neurofibromatosis type 2 gene product

B. S. Kang, D. R. Cooper, Y. Devedjiev, U. Derewenda and Z. S. Derewenda

Synopsis: The crystal structure of the FERM domain of merlin has been solved by molecular replacement and refined to 1.8 Å resolution. Missense mutations causing neurofibromatosis type 2 are examined.

PDB reference: 1h4r

Online 21 February 2002

 

Acta Cryst. (2002). D58, 392-397  [ doi:10.1107/S0907444901021187 ]

Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein

M. H. Bucher, A. G. Evdokimov and D. S. Waugh

Synopsis: Five small affinity tags had differing effects on the crystallization of P. furiosus maltodextrin-binding protein and the quality of the crystals that were obtained.

PDB reference: 1elj

Online 21 February 2002

 

Acta Cryst. (2002). D58, 398-406  [ doi:10.1107/S090744490200015X ]

Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis

A. G. Evdokimov, J. E. Tropea, K. M. Routzahn and D. S. Waugh

Synopsis: The crystal structure of the Y. pestis type III secretion chaperone SycE has been determined at a resolution of 1.95 Å.

PDB reference: 1k6z

Online 21 February 2002

 

Acta Cryst. (2002). D58, 407-413  [ doi:10.1107/S0907444901021278 ]

The structure of S100A12 in a hexameric form and its proposed role in receptor signalling

O. V. Moroz, A. A. Antson, E. J. Dodson, H. J. Burrell, S. J. Grist, R. M. Lloyd, N. J. Maitland, G. G. Dodson, K. S. Wilson, E. Lukanidin and I. B. Bronstein

Synopsis: The structure of a hexameric form of S100A12, a member of the S100 family of proteins, has been solved at 2.7 Å resolution. The results suggest a functional significance for the hexamer.

PDB reference: 1gqm

Online 21 February 2002

 

Acta Cryst. (2002). D58, 414-420  [ doi:10.1107/S0907444901021497 ]

Re-refinement using reprocessed data to improve the quality of the structure: a case study involving garlic lectin

G. Ramachandraiah, N. R. Chandra, A. Surolia and M. Vijayan

Synopsis: The resolution and the definition of the structure of garlic lectin could be improved by re-refinement using reprocessed data employing different program packages. The re-refined structure, amongst other things, leads to a better identification of residues at the variable locations in the sequence and hence of isolectins.

PDB reference: 1kj1

Online 21 February 2002

 

Acta Cryst. (2002). D58, 421-430  [ doi:10.1107/S0907444901021692 ]

The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis

C. A. Dennis, N. M. Glykos, M. R. Parsons and S. E. V. Phillips

Synopsis: The crystal structure of apo-AhrC, the hexameric arginine repressor/activator protein from B. subtilis, has been determined. The structure has been compared with previous 30 Å resolution EM studies of the protein and with crystal structures of its homologues from E. coli and B. stearothermophilus.

PDB reference: 1f9n

Online 21 February 2002

    

Acta Cryst. (2002). D58, 431-440  [ doi:10.1107/S0907444901021709 ]

Description of ordered solvent molecules in a platinated decanucleotide duplex refined at 1.6 Å resolution against experimental MAD phases

F. Coste, W. Shepard and C. Zelwer

Synopsis: MAD phases have been combined with the structure-factor magnitudes in the refinement by REFMAC of a platinated decanucleotide. They contributed significantly to the determination of the structure of the ordered water molecules and of a spermine molecule involved in intermolecular contacts.

NDB reference: DDJ075

Online 21 February 2002

 

Acta Cryst. (2002). D58, 441-450  [ doi:10.1107/S0907444901021758 ]

Atomic resolution structures of ribonuclease A at six pH values

R. Berisio, F. Sica, V. S. Lamzin, K. S. Wilson, A. Zagari and L. Mazzarella

Synopsis: Six structures of bovine pancreatic ribonuclease at six pH values have been refined and analyzed. A comparative analysis of the six models and some biological implications are discussed.

PDB references: 1kf2, 1kf3, 1kf4, 1kf5, 1kf7 and 1kf8

Online 21 February 2002

 

Acta Cryst. (2002). D58, 451-455  [ doi:10.1107/S0907444901021825 ]

Structure of a Cys25Ser mutant of human cathepsin S

J. P. Turkenburg, M. B. A. C. Lamers, A. M. Brzozowski, L. M. Wright, R. E. Hubbard, S. L. Sturt and D. H. Williams

Synopsis: The preparation and crystal structure determination of the active-site Cys25Ser mutant of human cathepsin S at 2.2 Å resolution is described. This structure clearly defines both the catalytic triad and the substrate-binding region.

PDB reference: 1glo

Online 21 February 2002

 

Acta Cryst. (2002). D58, 456-458  [ doi:10.1107/S0907444902000136 ]

Resolution improvement from `in situ annealing' of copper nitrite reductase crystals

M. J. Ellis, S. Antonyuk and S. S. Hasnain

Synopsis: The resolution of copper nitrite reductase crystals has been improved to 1 Å through a simple procedure of `in situ' annealing.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 459-471  [ doi:10.1107/S0907444902000112 ]

Flash-cooling and annealing of protein crystals

S. Kriminski, C. L. Caylor, M. C. Nonato, K. D. Finkelstein and R. E. Thorne

Synopsis: X-ray imaging and diffraction illuminate the character and origin of protein crystal disorder created by flash-cooling and how annealing can reduce this disorder. Annealing at fixed temperatures well below 273 K should provide a reliable low-risk approach for reducing cooling damage in more disordered crystals.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 472-479  [ doi:10.1107/S0907444902000124 ]

X-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins

D. Vivarès and F. Bonneté

Synopsis: The results from this small-angle scattering study have been extended to the crystallization of large proteins in the presence of polyethylene glycol. The protein crystallization, the nucleation rate and the different morphological crystal shapes obtained were correlated with the second virial coefficient.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 480-486  [ doi:10.1107/S0907444902000616 ]

A novel pH-dependent dimerization motif in -lactoglobulin from pig (Sus scrofa)

F. J. Hoedemaeker, R. W. Visschers, A. C. Alting, K. G. de Kruif, M. E. Kuil and J. P. Abrahams

Synopsis: The structure of porcine -lactoglobulin shows a novel and unusual dimerization motif not previously seen in members of the lipocalin family. This partially explains the markedly different physicochemical properties of porcine and bovine -lactoglobulin, despite these proteins sharing 66% amino-acid identity.

PDB reference: 1exs

Online 21 February 2002

 

Acta Cryst. (2002). D58, 487-493  [ doi:10.1107/S0907444902000525 ]

Pattern-recognition methods to identify secondary structure within X-ray crystallographic electron-density maps

T. Oldfield

Synopsis: A pattern-recognition search algorithm is described that interprets X-ray electron-density maps and forms the initial stage in automated electron-density map interpretation.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 494-506  [ doi:10.1107/S090744490200118X ]

Jolly SAD

Z. Dauter, M. Dauter and E. J. Dodson

Synopsis: Numerous examples show that with accurate diffraction data SAD phasing leads to a rapid solution of macromolecular crystal structures.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 507-510  [ doi:10.1107/S0907444901021266 ]

Crystallization and preliminary X-ray diffraction analysis of L-aminoacylase from the hyperthermophilic archaeon Thermococcus litoralis

E. J. Hollingsworth, M. N. Isupov and J. A. Littlechild

Synopsis: Rhombohedral crystals of L-aminoacylase from T. litoralis have been grown by the sitting-drop vapour-diffusion technique from recombinant protein expressed in E. coli. The crystals show diffraction to 2.8 Å resolution. The position of the zinc ion has been located using the anomalous data.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 511-512  [ doi:10.1107/S0907444901021461 ]

Crystallization of the Oct-1/SNAP190 peptide/DNA complex

S. Hovde, A. Brooks, K. Strong and J. H. Geiger

Synopsis: Crystallization and preliminary diffraction results for the Oct-1/SNAP190 peptide/DNA complex are presented.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 513-514  [ doi:10.1107/S0907444902000276 ]

Crystallization and preliminary X-ray diffraction studies of human angiostatin

M. C. Abad and J. Geiger

Synopsis: The angiogenesis inhibitor angiostatin has been crystallized and a complete data set to 1.75 Å resolution has been collected. The crystals belong to the P4₁2₁2 space group, with unit-cell parameters a = b = 56.94, c = 192.97 Å.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 515-518  [ doi:10.1107/S090744490102145X ]

Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae

K. Steinhauer, G. S. Allen, W. Hillen, J. Stülke and R. G. Brennan

Synopsis: The M. pneumoniae HPr kinase/phosphatase (HPrK/P) was crystallized in the space group P2₁2₁2₁, with unit-cell parameters a = 117.1, b = 127.7, c = 170.7 Å. Both X-ray and biophysical data indicate that HPrK/P is a functional hexamer that undergoes an ATP-binding-induced conformational change.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 519-521  [ doi:10.1107/S090744490102159X ]

Cloning, purification, crystallization and preliminary X-ray studies of RFC boxes II-VIII of replication factor C from Methanococcus jannaschii

I. Lee, N. K. Lokanath, K. Min, S. C. Ha, D. Y. Kim and K. K. Kim

Synopsis: RFC boxes II-VIII of replication factor C from M. jannaschii have been crystallized and native data have been collected at 3.2 Å resolution using synchrotron X-rays.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 522-523  [ doi:10.1107/S0907444901021710 ]

Crystallization and preliminary X-ray diffraction analysis of cytochrome c peroxidase from the purple phototrophic bacterium Rhodobacter capsulatus

L. De Smet, D. Leys and J. Van Beeumen

Synopsis: Crystallogenesis and diffraction to a resolution of 2.7 Å are described for the dihaem cytochrome c peroxidase of R. capsulatus, the first example of this type of enzyme isolated from a phototrophic bacterium.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 524-525  [ doi:10.1107/S0907444901021874 ]

Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF

C. Rosano, S. Zuccotti, M. Stefani, M. Bucciantini, G. Ramponi and M. Bolognesi

Synopsis: The prokaryotic hydrogenase maturation factor protein HypF (82 kDa) contains a 10 kDa domain displaying structural homology to prokaryotic and eukaryotic acylphosphatases. Two different crystal forms of the HypF N-terminal domain have been characterized.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 526-528  [ doi:10.1107/S0907444902000768 ]

Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH₂ppA

S. Bailey, S. E. Sedelnikova, G. M. Blackburn, H. M. Abdelghany, A. G. McLennan and J. B. Rafferty

Synopsis: The diadenosine tetraphosphate hydrolase from C. elegans has been crystallized in the presence of a substrate analogue. The crystals belong to space group P2₁ and diffract to 2.0 Å resolution.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 529-530  [ doi:10.1107/S0907444902001063 ]

Crystallization and synchrotron X-ray diffraction studies of human interleukin-22

R. A. P. Nagem, K. W. Lucchesi, D. Colau, L. Dumoutier, J.-C. Renauld and I. Polikarpov

Synopsis: The preliminary X-ray analysis of recombinant human interleukin-22, a novel member of the cytokine family, is reported.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 531-532  [ doi:10.1107/S0907444902000227 ]

Crystallization and preliminary X-ray crystallographic analysis of -xylosidase from Thermoanaerobacterium saccharolyticum, a thermophilic anaerobe

J. K. Yang, H.-J. Yoon, H. J. Ahn, B. I. Lee, H.-W. Kim, M. Laivenieks, C. Vieille, J. G. Zeikus and S. W. Suh

Synopsis: -Xylosidase from the thermophilic anaerobe T. saccharolyticum has been crystallized at 296 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.4 Å resolution with synchrotron X-rays.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 533-535  [ doi:10.1107/S0907444902000264 ]

Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex

J.-P. Himanen and D. B. Nikolov

Synopsis: Recombinant EphB2/ephrin-B2 receptor-ligand complex has been purified, biochemically characterized and studied for crystallization conditions. Of the two different cocrystal forms generated, one is suitable for X-ray diffraction studies.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 536-538  [ doi:10.1107/S0907444902000203 ]

Expression, purification, refolding and crystallization of the carbohydrate-recognition domain of p58/ERGIC-53, an animal C-type lectin involved in export of glycoproteins from the endoplasmic reticulum

L. M. Velloso, K. Svensson, U. Lahtinen, G. Schneider, R. F. Pettersson and Y. Lindqvist

Synopsis: The carbohydrate-recognition domain of p58 was produced in insect cells and in E. coli, purified and crystallized using Li₂SO₄ as a precipitant. Crystals belong to the space group I222, with unit-cell parameters a = 49.6, b = 86.1, c = 128.1 Å and one molecule per asymmetric unit. These crystals diffract to at least 1.46 Å resolution.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 539-541  [ doi:10.1107/S0907444902000239 ]

Crystallization and preliminary X-ray analysis of the ATP-binding domain of the ABC transporter haemolysin B from Escherichia coli

L. Kránitz, H. Benabdelhak, C. Horn, M. A. Blight, I. B. Holland and L. Schmitt

Synopsis: Crystallization and preliminary analysis of the ATPase domain of the ABC transporter HlyB from E. coli are described.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 542-545  [ doi:10.1107/S0907444902000355 ]

Crystallization and X-ray analysis of native and selenomethionyl -mannanase Man5A from blue mussel, Mytilus edulis, expressed in Pichia pastoris

B. Xu, I. G. Muñoz, J.-C. Janson and J. Ståhlberg

Synopsis: About 40% incorporation of SeMet in Man5A -mannanase from blue mussel, M. edulis, was obtained with the commercial P. pastoris expression system. The presence of selenium in the crystals was confirmed by an X-ray fluorescence scan. Diffraction to 1.5 Å has been obtained.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 546-548  [ doi:10.1107/S0907444902001245 ]

Thermophilic alcohol dehydrogenase from the mesophile Entamoeba histolytica: crystallization and preliminary X-ray characterization

L. J. W. Shimon, M. Peretz, E. Goihberg, Y. Burstein and F. Frolow

Synopsis: Alcohol dehydrogenase from the protozoan parasite E. histolytica has been crystallizaed in space group C222₁ with unit-cell parameters a = 76.89, b = 234.24, c = 96.24 Å and a dimer per asymmetric unit. The crystals diffract to 1.9 Å.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 549-552  [ doi:10.1107/S0907444902000148 ]

Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase

C. Momany, V. Levdikov, L. Blagova and K. Crews

Synopsis: Diaminopimelate decarboxylase from E. coli was cloned, expressed, purified and crystallized. Large well ordered crystals diffract to at least 2.1 Å and belong to space group P6₁22, with unit-cell parameters a = b = 98.6, c = 177 Å.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 553-555  [ doi:10.1107/S0907444902001427 ]

Crystallization and preliminary X-ray diffraction studies of a D-lysine-based chiral PNA-DNA duplex

V. Menchise, G. De Simone, R. Corradini, S. Sforza, N. Sorrentino, A. Romanelli, M. Saviano and C. Pedone

Synopsis: The crystallization of a chiral PND-DNA duplex is reported. Synchrotron X-ray radiation was used to collect diffraction data to 1.85 Å resolution.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 556-558  [ doi:10.1107/S0907444902000537 ]

Expression, crystallization and preliminary X-ray diffraction studies on the complete choline-binding domain of the major pneumococcal autolysin

C. Fernández-Tornero, A. Ramón, C. Fernández-Cabrera, G. Giménez-Gallego and A. Romero

Synopsis: In order to confirm the hypothesis that the previously reported C-terminal fragment of the major pneumococcal autolysin was not the complete choline-binding domain of this enzyme, the full-length C-terminal domain has been crystallized. Diffraction data to 3.2 Å resolution allowed the determination of the space group (P2₁) and the unit-cell parameters (a = 51.9, b = 30.3, c = 113.6 Å, = 96.4°).

Online 21 February 2002

 

Acta Cryst. (2002). D58, 559-561  [ doi:10.1107/S0907444902001233 ]

Crystallization and preliminary X-ray diffraction analysis of chloroplastic ascorbate peroxidase of tobacco plants

K. Wada, T. Tada, Y. Nakamura, Y. Yabuta, K. Yoshimura, T. Takeda, S. Shigeoka and K. Nishimura

Synopsis: Ascorbate peroxidase from tobacco plants has been purified and crystallized in the orthorhombic space group P2₁2₁2₁. A native data set has been collected to 1.6 Å resolution using the KEK-PF synchrotron-radiation source.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 562-563  [ doi:10.1107/S0907444902001415 ]

Crystallization and preliminary X-ray crystallographic analysis of malonamidase E2, an amidase signature family member

S. Shin, T.-H. Lee, H. M. Koo, S. Kim, H.-S. Lee, Y. S. Kim and B.-H. Oh

Synopsis: Malonamidase E2, an amidase signature family member, was crystallized and analyzed by X-ray crystallographic methods at a preliminary level.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 564-566  [ doi:10.1107/S0907444902001403 ]

Crystallization and preliminary X-ray crystallographic analysis of SEDL

S. B. Jang, Y.-S. Cho, S.-J. Eom, E.-J. Choi, K.-H. Kim, P.-G. Suh and B.-H. Oh

Synopsis: SEDL with a putative role in ER-to-Golgi transport has been overexpressed, crystallized, and analyzed by X-ray crystallographic method at a preliminary level.

Online 21 February 2002

 

Acta Cryst. (2002). D58, 567-569  [ doi:10.1107/S0907444902001555 ]

Structural characterization of a new crystal form of the four-way Holliday junction formed by the DNA sequence d(CCGGTACCGG)₂: sequence versus lattice?

J. H. Thorpe, S. C. M. Teixeira, B. C. Gale and C. J. Cardin

Synopsis: A new crystal form of the DNA Holliday junction is formed by d(CCGGTACCGG)₂ which allows the effects of sequence and lattice type on junction geometry to be distinguished.

NDB reference: ud0015

Online 21 February 2002