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The structure-based fragment-assembly approach described in the present study facilitated the rapid identification and subsequent synthesis of caspase-1 inhibitors with cell-based activity and provided insights into the enzyme’s ability to accommodate different inhibitor-binding modes in the active site.
The crystal structure of purine nucleoside phosphorylase (DeoD) from B. anthracis was solved by X-ray crystallography using molecular replacement and refined at a resolution of 2.24 Å.
The structure of P. horikoshii OT3 protein PH0500 was determined by the multiple anomalous dispersion method and refined in two crystal forms. The protein is a dimer and has a PIN-domain fold.
The crystal structure of the 37.2 kDa At3g21360 gene product from A. thaliana was determined at 2.4 Å resolution. The structure establishes that this protein binds a metal ion and is a member of a clavaminate synthase-like superfamily in A. thaliana.
Chorismate mutase from M. tuberculosis has been crystallized. Preliminary X-ray crystallographic studies reveal the occurrence of a dimeric molecule in the crystal asymmetric unit.
The expression, purification and preliminary X-ray diffraction studies of a chitin-binding domain of the chitinase from P. furiosus are reported.
A novel thermoalkalophilic depolymerase, PhaZ7, from P. lemoignei was crystallized by the microdialysis technique. Crystals belong to space group C2 and diffract to 2.75 Å resolution at a synchrotron source.
Two crystal forms of the aconitase version of recombinant human IRP1 are reported.
Yeast NAD+-isocitrate dehydrogenase has been purified and crystallized using sodium citrate, a competitive inhibitor of the enzyme, as a precipitant. Preliminary X-ray analyses indicate the molecular boundaries of the molecule and large continuous solvent channels in the crystal.
Single crystals of the holoenzyme (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase with ThDP and Mn2+ as cofactors were obtained by the hanging-drop vapour-diffusion method with 35% ethylene glycol as precipitant. Apoenzyme crystals were obtained by sitting-drop vapour diffusion with 70% MPD.
The first crystallographic study of a member of the YaeQ family of proteins, which are conserved in a small group of Gram-negative bacteria, most of which are animal or plant pathogens, is reported. Diffraction data were collected to 1.9 Å resolution and an interpretable electron-density map was obtained.
B. subtilis YjcG protein was expressed, purified and crystallized. A complete diffraction data set was collected at BSRF beamline 3W1A and processed to 2.3 Å resolution.
The crystallization of recombinant bovine uteroglobin.
Ferritin from P. furiosus crystallizes in space group C2221, with unit-cell parameters a = 258.1, b = 340.1, c = 266.5 Å and 36 monomers in the asymmetric unit, corresponding to one and a half 24-mers.
The Holliday junction resolvase of the archaeal virus SIRV2 infecting the archaeon Sulfolobus islandicus has been crystallized and a full data set has been collected at 3.4 Å resolution. Analysis of the self-rotation function suggests the presence of two dimers in the asymmetric unit with a solvent content of 77%.
The expression, purification, crystallization and preliminary X-ray diffraction studies of mouse centrin1 are reported.
A presequence peptide derived from rat aldehyde dehydrogenase was tethered to the cytosolic domain of rat Tom20 protein via an intermolecular disulfide bond. Two crystal forms were obtained with different linker designs and diffracted to 2.1 and 1.9 Å.
Mycobacterial PimA is an essential enzyme that catalyses the first mannosylation step in phosphatidyl-myo-inositol mannoside (PIM) biosynthesis. Crystals of the enzyme from M. smegmatis, obtained in the presence of GDP and myo-inositol, are orthorhombic (P212121) and diffract X-rays to 2.4 Å resolution.
Recombinant human E1 enzyme has been crystallized using the hanging-drop vapour-diffusion method and diffraction-quality crystals were grown at 291 K using PEG 4000 as precipitant.
Two different fragments of the ligand-binding domain of LOX-1, the major receptor for oxidized low-density lipoprotein (LDL) on endothelial cells, have been crystallized in different forms.
The water-forming flavoenzyme NADH oxidase was crystallized successfully for the first time. The crystals diffract X-rays to at least 4.0 Å resolution.
Crystallization of human enhancer of rudimentary homologue protein.
The gene encoding the unusual metal-ion-dependent epoxidase involved in fosfomycin biosynthesis, S. wedmorensis (S)-2-hydroxypropylphosphonic acid epoxidase, has been cloned and the protein expressed, purified and crystallized. Two crystal forms have been obtained, one of which diffracts to high resolution.
Strongly diffracting crystals of a methanol-induced corrinoid protein from M. thermoacetica have been obtained.