Structural Biology and Crystallization Communications

 

Acta Cryst. (2005). F61, 258-262  [ doi:10.1107/S1744309105002435 ]

Two crystal structures of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveal protein-ligand interactions including a structural basis for observed antifolate resistance

A. C. Anderson

Synopsis: An analysis of the protein-ligand interactions in two crystal structures of DHFR-TS from C. hominis reveals a possible structural basis for observed antifolate resistance in C. hominis DHFR. A comparison with the structure of human DHFR reveals residue substitutions that may be exploited for the design of species-selective inhibitors.

PDB references: 1qzf and 1sej

Online 8 February 2005

 

Acta Cryst. (2005). F61, 263-265  [ doi:10.1107/S1744309105004823 ]

X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site

A. C. Rufer, L. Thiebach, K. Baer, H. W. Klein and M. Hennig

Synopsis: The crystal structure of the 26 kDa glutathione S-transferase from S. japonicum (SjGST) was determined at 3 Å resolution in the new space group P2₁2₁2₁. The structure of orthorhombic SjGST reveals unique features of the ligand-binding site and dimer interface when compared with previously reported structures.

PDB reference: 1y6e

Online 24 February 2005

 

Acta Cryst. (2005). F61, 266-268  [ doi:10.1107/S1744309105002265 ]

Preliminary crystallographic analysis of ADP-glucose pyrophosphorylase from Agrobacterium tumefaciens

J. R. Cupp-Vickery, R. Y. Igarashi and C. R. Meyer

Synopsis: Crystallization and X-ray diffraction methods for native A. tumefaciens ADP-glucose pyrophosphorylase and its selenomethionyl derivative are described. Two crystal forms are identified, both of which diffract to 2 Å.

Online 8 February 2005

 

Acta Cryst. (2005). F61, 269-270  [ doi:10.1107/S174430910500223X ]

Cloning, purification, crystallization and preliminary crystallographic analysis of a hypothetical acetyltransferase from Pyrococcus furiosus

S. Biarrotte-Sorin and C. Mayer

Synopsis: The crystallization of a hypothetical acetyltransferase from the archaeon P. furiosus by hanging-drop vapour diffusion is reported in space group P622.

Online 8 February 2005

 

Acta Cryst. (2005). F61, 271-273  [ doi:10.1107/S1744309105002472 ]

Purification, crystallization and preliminary crystallographic analysis of DehIVa, a dehalogenase from Burkholderia cepacia MBA4

J. W. Schmidberger, A. J. Oakley, J. S. H. Tsang and M. C. J. Wilce

Synopsis: The dhlIVa gene coding for DehIVa was expressed in Escherichia coli and the protein was purified and crystallized using the hanging-drop method.

Online 8 February 2005

 

Acta Cryst. (2005). F61, 274-278  [ doi:10.1107/S1744309105002678 ]

Crystallization of a truncated soluble human semicarbazide-sensitive amine oxidase

E. Jakobsson, J. Nilsson, U. Källström, D. Ogg and G. J. Kleywegt

Synopsis: A truncated soluble human semicarbazide-sensitive amine oxidase has been crystallized. Data were collected to 2.5 Å from a crystal suffering from twinning, pseudo-symmetry and anisotropy. The structure was solved in space group P4₃.

Online 8 February 2005

 

Acta Cryst. (2005). F61, 279-281  [ doi:10.1107/S174430910500285X ]

Expression, purification, crystallization and preliminary X-ray crystallographic studies of a cold-adapted aspartate carbamoyltransferase from Moritella profunda

D. De Vos, P. Hulpiau, B. Vergauwen, S. N. Savvides and J. Van Beeumen

Synopsis: Crystals of the aspartate carbamoyltransferase of the psychrophile M. profunda diffract X-rays to 2.85 Å. Three catalytic and three regulatory subunits are predicted per asymmetric unit.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 282-284  [ doi:10.1107/S1744309105002861 ]

Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein TXNL4B

T. Jin, A. J. Howard, E. A. Golemis, Y. Wang and Y.-Z. Zhang

Synopsis: Human spliceosomal protein TXNL4B was purified and crystallized.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 285-287  [ doi:10.1107/S1744309105002988 ]

Crystallization and preliminary X-ray structural studies of a high-affinity CD8 co-receptor to pMHC

D. K. Cole, P. J. Rizkallah, M. Sami, N. M. Lissin, F. Gao, J. I. Bell, J. M. Boulter, M. Glick, A. Vuidepot, B. K. Jakobsen and G. F. Gao

Synopsis: A high-affinity mutant CD8 (haCD8) has been developed with the aim of developing a therapeutic immunosuppressor. In order to fully understand the nature of the haCD8 interaction, this protein was crystallized using the sitting-drop vapour-diffusion method.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 288-290  [ doi:10.1107/S174430910500299X ]

Crystallization and preliminary X-ray analysis of alginate lyases A1-II and A1-II' from Sphingomonas sp. A1

M. Yamasaki, K. Ogura, S. Moriwaki, W. Hashimoto, K. Murata and B. Mikami

Synopsis: The crystallization and preliminary characterization of the family PL-7 alginate lyases A1-II and A1-II' from Sphingomonas sp. A1 are presented.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 291-292  [ doi:10.1107/S1744309105003635 ]

Crystallization and preliminary X-ray analysis of reducing-end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125

Y. Honda, S. Fushinobu, M. Hidaka, T. Wakagi, H. Shoun and M. Kitaoka

Synopsis: Reducing-end-xylose releasing exo-oligoxylanase (Rex) from B. halodurans C-125 was crystallized. A diffraction data set was collected to 1.35 Å resolution.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 293-295  [ doi:10.1107/S1744309105003659 ]

Crystallization and preliminary X-ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilus

H. Chon, H. Matsumura, Y. Koga, K. Takano and S. Kanaya

Synopsis: A thermostable ribonuclease HIII from B. stearothermophilus (Bst RNase HIII) was crystallized and preliminary crystallographic studies were performed. Plate-like overlapping polycrystals were grown by the sitting-drop vapour-diffusion method at 283 K.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 296-298  [ doi:10.1107/S1744309105003611 ]

Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor SelB in complex with RNA

L. Rasubala, D. Fourmy, T. Ose, D. Kohda, K. Maenaka and S. Yoshizawa

Synopsis: The mRNA-binding domain of M. thermoacetica selenocysteine-specific elongation factor SelB (residues 512-634, SelB-M) was overproduced in E. coli and its cognate mRNA ligand, 23 nucleotides of the SECIS RNA hairpin, was chemically prepared. The purified SelB-M-SECIS RNA complex has been crystallized in space group P2₁2₁2 and diffracted to 2.3 Å.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 299-301  [ doi:10.1107/S174430910500374X ]

Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus

O. Einsle, H. Niessen, D. J. Abt, G. Seiffert, B. Schink, R. Huber, A. Messerschmidt and P. M. H. Kroneck

Synopsis: Acetylene hydratase, a tungsten-containing hydroxylase that converts acetylene to acetaldehyde, has been purified and crystallized under anaerobic conditions.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 302-304  [ doi:10.1107/S1744309105003842 ]

Crystallization and preliminary X-ray analysis of Thermoactinomyces vulgaris R-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylase

K. Ichikawa, T. Tonozuka, M. Mizuno, Y. Tanabe, S. Kamitori, A. Nishikawa and Y. Sakano

Synopsis: A maltooligosaccharide-metabolizing enzyme from T. vulgaris R-47 (TGA) homologous to glucoamylase degrades maltooligosaccharides more efficiently than starch, unlike fungal glucoamylases. TGA was crystallized and the state of the protein in solution was analyzed by gel-filtration chromatography.

Online 12 February 2005

 

Acta Cryst. (2005). F61, 305-307  [ doi:10.1107/S1744309105003945 ]

Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli

S. G. Addinall, K. A. Johnson, T. Dafforn, C. Smith, A. Rodger, R. P. Gomez, K. Sloan, A. Blewett, D. J. Scott and D. I. Roper

Synopsis: An open reading frame from E. coli MG1655 has been cloned, expressed and purified. Crystals obtained from the purified recombinant protein have been obtained in a variety of different forms diffracting to 1.8 Å resolution.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 308-311  [ doi:10.1107/S1744309105004082 ]

Crystallization and preliminary X-ray crystallographic studies of a psychrophilic subtilisin-like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS-11

D. Dong, T. Ihara, H. Motoshima and K. Watanabe

Synopsis: The psychrophilic protease Apa1 consisting of a subtilisin-like region and a large insert (148 residues) with unknown structure has been crystallized. Collection of a data set to 1.78 Å resolution and molecular-replacement searches are reported.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 312-314  [ doi:10.1107/S1744309105004367 ]

Crystallization and preliminary X-ray crystallographic analysis of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA-1

W. Oonanant, J. Sucharitakul, J. Yuvaniyama and P. Chaiyen

Synopsis: This paper describes the first crystallization study of a flavoprotein monooxygenase that can cleave an aromatic compound without requiring a metal-ion cofactor.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 315-318  [ doi:10.1107/S1744309105005014 ]

Expression, purification, crystallization and preliminary X-ray studies of the outer membrane efflux proteins OprM and OprN from Pseudomonas aeruginosa

I. Broutin, H. Benabdelhak, X. Moreel, M.-B. Lascombe, D. Lerouge and A. Ducruix

Synopsis: Two outer membrane factor family proteins, OprM and OprN, from a tripartite efflux pump found in P. aeruginosa were crystallized. A diffraction data set was collected to 3.8 Å resolution in the space group C2 for OprM crystals.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 319-322  [ doi:10.1107/S1744309105005269 ]

Overproduction and preliminary crystallographic study of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3

H. Chon, H. Matsumura, S. Shimizu, N. Maeda, Y. Koga, K. Takano and S. Kanaya

Synopsis: A human kynurenine aminotransferase II homologue from P. horikoshii OT3 has been overproduced in E. coli, purified, and characterized. Crystals of this protein have been obtained and analyzed by X-ray diffraction.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 323-325  [ doi:10.1107/S1744309105005294 ]

Crystallization and preliminary X-ray diffraction analysis of thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1

T. Nakamura, H. Matsumura, T. Inoue, Y. Kai, K. Uegaki, Y. Hagihara, M. Ataka and K. Ishikawa

Synopsis: The hyperthermostable thioredoxin peroxidase from the aerobic hyperthermophilic archaeon A. pernix K1 was crystallized. The crystal diffracted to 2.7 Å resolution.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 326-331  [ doi:10.1107/S1744309105004835 ]

Energetics of 5-bromo-4-chloro-3-indolyl--D-mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing

F. Gallego del Sol, J. Gómez, S. Hoos, C. S. Nagano, B. S. Cavada, P. England and J. J. Calvete

Synopsis: The first crystal structure of a Mimosoideae lectin, Parkia platycephala has been solved by MAD phasing using 5-bromo-4-chloro-3-indolyl--D-mannose as an anomalous X-ray scatterer. This strategy may be useful for structure elucidation of novel lectins or when molecular replacement methods fail.

Online 24 February 2005

 

Acta Cryst. (2005). F61, 332-334  [ doi:10.1107/S174430910500309X ]

Crystallization and preliminary crystallographic analysis of the site-specific DNA nickase Nb.BspD6I

G. S. Kachalova, E. A. Rogulin, R. I. Artyukh, T. A. Perevyazova, L. A. Zheleznaya, N. I. Matvienko and H. D. Bartunik

Synopsis: The site-specific DNA nickase Nb.BspD6I has been crystallized in space group P2₁, with unit-cell parameters a = 57.76, b = 90.67, c = 71.71, = 110.1°.

Online 1 March 2005

 

Acta Cryst. (2005). F61, 335-336  [ doi:10.1107/S1744309105004057 ]

Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1

K. D'Ambrosio, G. De Simone, E. Pedone, M. Rossi, S. Bartolucci and C. Pedone

Synopsis: A protein disulfide oxidoreductase from A. pernix K1 has been crystallized for the first time. The crystals belong to space group I222 or I2₁2₁2₁ and diffract to 1.93 Å resolution.

Online 1 March 2005