|Home | About | Journals | Submit | Contact Us | Français|
The structures of thioredoxins from several species, including man and E. coli, are known. The bacterium S. coelicolor contains three thioredoxins with unknown physiological functions. TrxA from S. coelicolor has been overexpressed, purified and crystallized and its crystal structure determined at 1.5 Å resolution.
The crystal structure of human factor VIIa/soluble tissue factor in complex with a highly selective peptide-mimetic factor VIIa inhibitor has been solved at 2.6 Å resolution. This structure suggests that Asp60 and Lys192 are key residues for achieving high selectivity against thrombin inhibition.
The major SH2-binding site of p130Cas has been crystallized in complex with the SH3-SH2 regulatory domains of the Src-family kinase Lck.
α-Xylosidase from E. coli has been crystallized in space group P212121.
Crystallization and preliminary X-ray analysis of the CphA metallo-β-lactamase from A. hydrophilia are described. The crystals belonged to space group P21212, with unit-cell parameters a = 40.75, b = 42.05, c = 128.88 Å, and diffract to 1.8 Å.
Mlc, a transcriptional regulator from E. coli, has been expressed, purified and crystallized. Diffraction data were collected to 2.9 Å from an Se-derivative crystal.
Crystals of Pru av 2, the first allergenic thaumatin-like protein, have been obtained and diffracted to 1.6 Å at a synchrotron. Using an annealing protocol, the resolution limit was improved to 1.3 Å:
The isolation, characterization and preliminary crystallographic studies of two new toxic PLA2s from the venom of V. nikolskii, which has only recently been established as a new species, are reported.
The biotin–protein ligase from P. horikoshii OT3 was overexpressed, purified, crystallized and cocrystallized with biotin, ADP and biotinyl-5′-AMP. The crystals belong to space group P21 and diffract to beyond 1.6 Å resolution.
Crystallization of a fructosyl amino acid oxidase from Corynebacterium sp. 2-4-1 yields two forms: one monoclinic and one tetragonal.
Glutamate racemase from L. fermenti has been overexpressed and crystallized. Diffraction data have been collected to beyond 2.28 Å resolution using a synchrotron-radiation source.
Sepiapterin reductase from C. tepidum has been crystallized by the hanging-drop vapour-diffusion method. Phasing information has been obtained experimentally by MAD using a SeMet derivative.
Blue laccase from the white-rot basidiomycete P. tigrinus, an enzyme involved in lignin biodegradation, has been crystallized. The crystals obtained give diffraction data at 1.4 Å, the best resolution to date for this class of enzymes, which may assist in further elucidation of the catalytic mechanism of multicopper oxidases.
PAB0955 has been expressed, purified and crystallized, and it has been shown that this thermostable protein is dimeric in reductive conditions.
Mimivirus, the largest known double-stranded DNA virus, unexpectedly exhibits components of the protein-translation apparatus. The crystallization and functional assay of the viral tyrosyl tRNA synthetase are reported.
Human cyclophilin J is a member of the cyclophilin family and recent studies have indicated that it plays a role in the formation of liver cancers as a regulation factor or messenger. The preparation, crystallization and preliminary X-ray crystallographic studies of human cyclophilin J are reported.
Crystallization, data collection and initial structure determination of a mesophilic family 11 xylanase from B. subtilis 1A1 are reported.
The modular choline-binding protein Pce, the phosphorylcholine esterase from S. pneumoniae, has been crystallized by the hanging-drop vapour-diffusion method. A SAD data set from a derivative with a gadolinium complex has been collected to 2.7 Å resolution.
An N-terminal construct of mDia1, a member of the diaphanous-related formin family, was overexpressed, purified and crystallized in complex with RhoC. Data collection from native and SeMet crystals is reported.
Plasmepsin 4 from the malarial parasite P. malariae has been crystallized in complex with a small molecular inhibitor. Preliminary X-ray analysis of the diffraction data collected at 3.3 Å resolution is reported.
Fel d 1, a major allergen from cat, has been expressed, purified and crystallized. The crystals belong to space group P1 and diffract to 1 Å resolution.
The crystallization of the enzyme ‘modulator of drug activity B’ (MdaB) from E. coli, which has activity similar to that of mammalian DT-diaphorase, is presented.
Three paralogues of a deblocking aminopeptidase from the hyperthermophilic archeon P. horikoshii have been overexpressed in E. coli, purified and crystallized and exist in different oligomeric states.
The C-terminal domain of Rv2874, the DipZ homologue from M. tuberculosis, has been expressed, purified and crystallized.
A homo-tetrameric psychrophilic alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123 has been crystallized. Its molecular structure is under investigation.
A predicted protein module BIV2-Helix of BIVgp40 has been expressed in Escherichia coli and purified by chromatography. Recombinant BIV2-Helix was crystallized using the hanging-drop vapour-diffusion technique at 291 K.
The cellulose biosynthesis-related protein CMCax from A. xylinum has been purified and crystallized. The crystals of CMCax belong to the primitive hexagonal space group P61 or P65, with unit-cell parameters a = b = 89.1, c = 94.2 Å.
XynX, a family 10 xylanase from A. punctata ME-1, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to beyond 1.8 Å resolution.