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The crystal structure of the synthetase domain of human CTPS has been determined. The structure is the first of an eukaryotic CTPS and provides a starting point for drug design towards CTPS.
The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a —CF2— or —CHNH2— spacer group.
The structure of porcine pancreatic elastase at 1.5 Å resolution has a unique conformation induced by tris(hydroxymethyl)aminomethane as a buffer component.
Crystals of Stx2 were grown in the presence of adenosine and adenine. In both cases, the resulting electron density showed only adenine bound at the active site of the A subunit, proving that the holotoxin is an active N-glycosidase.
Human macrophage inflammatory protein-3α (MIP-3α) has been crystallized in a new space group I4. Crystals diffract to 1.81 Å.
The crystallization and preliminary X-ray characterization of a shikimate dehydrogenase from C. glutamicum is presented.
Crystals of a complex of the E. coli proteins BtuB (outer membrane cobalamin transporter) and TonB (carboxy-terminal domain) diffracting to 2.1 Å resolution have been obtained.
Crystals of a canonical inhibitor of plasmin from Australian Brown snake venom has been obtained. In complex with trypsin these diffract to 2.0 Å resolution, while the free inhibitor diffracts to 1.63 Å.
The crystallization and preliminary crystallographic analysis of a family GH78 α-l-rhamnosidase, RhaB from Bacillus sp. GL1, are presented.
Production, crystallization and phasing procedures are reported for the complex of human centrin 2, lacking the first 25 residues, and a 17-residue peptide from the protein XPC.
Human M-ficolin fibrinogen-like domain has been overexpressed in P. pastoris, purified and crystallized. Diffraction data have been collected to 1.9 Å.
The PIN domain of human EST1A was expressed, purified and crystallized by the sitting-drop vapour-diffusion method.
The metallo-glycerophosphodiesterase from E. aerogenes (GpdQ) has been cloned, expressed in E. coli and purified. Initial screening of crystallization conditions for this enzyme resulted in the identification of needles from one condition in a sodium malonate grid screen. Removal of the metals from the enzyme and subsequent optimization of these conditions led to crystals.
Crystals adequate for X-ray diffraction analysis have been prepared from L. interrogans ferredoxin-NADP+ reductase.
Locked nucleic acid (LNA) nucleotides are RNA analogues with a useful additional conformational constraint; the current investigation will provide the first crystallographic view of an all-LNA duplex.
The crystallization and preliminary X-ray crystallographic analysis of a protease inhibitor from the haemolymph of the Indian tasar silk worm A. mylitta is reported.
The choline-binding protein CbpI from S. pneumoniae has been purified and crystallized and diffraction data have been collected to 3.5 Å resolution.
The mature form of RafE has been expressed, purified and crystallized. X-ray diffraction data have been collected to 3.65 and 2.90 Å resolution from native and selenomethionine-derivative crystals, respectively.
The seed lectin from Lotus tetragonolobus (LTA) has been crystallized. The best crystals grew over several days and were obtained using the vapour-diffusion method at a constant temperature of 293 K.
Diffraction data from E. coli RNase II crystals of wild type and of an inactive mutant and its SeMet-derivative form were obtained to 2.44 and 2.74 Å resolution, providing a set of preliminary phases. An improved purification protocol allowed higher reproducibility in the crystallization of the mutant form.
Vascular apoptosis-inducing protein 1 (VAP1) and VAP2 from C. atrox venom were crystallized in variety of different crystal forms. Diffraction data sets were obtained to 2.5 and 2.15 Å resolution for VAP1 and VAP2, respectively.
Crystals of Rab11 in complex with the Rab-binding domain (RBD) of its effector Rab11-FIP2 were grown and synchrotron diffraction data were collected at 2.8 Å resolution.
The isolation, purification, crystallization and molecular-replacement solution of mitochondrial type II peroxiredoxin from P. sativum is reported.
E. coli aminopeptidase N has been crystallized by the vapour-diffusion method. Diffraction data have been collected and processed to 2.0 Å resolution.
DIR1, a putative LTP2 protein from Arabidopsis thaliana implicated in systemic acquired resistance in planta, has been crystallized in space group P212121 with one molecule per asymmetric unit.
Crystallization of a surface-localized acid phosphatase from Bacillus anthracis is reported. Flash annealing increased the high-resolution limit of usable data from 1.8 to 1.6 Å.
A corrigendum to the article by Hu et al. (2005), Acta Cryst. F61, 486–488.