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Apo and GDP-bound crystal structures of an essential GTPase, YsxC, from T. maritima were determined to maximal resolutions of 2.3 and 1.9 Å, respectively. Switch I in GDP–YsxC can adopt both an ‘open’ and ‘closed’ conformation, suggesting a mechanism for diffusion of GDP out of the nucleotide-binding pocket.
The 2.0 Å resolution crystal structure of tetrameric (αβ)2 R-state human adult aquomethemoglobin reveals axial water coordination at both the α and β heme sites.
The structure of a recombinant form of the sweet-tasting protein thaumatin I was determined at 1.1 Å resolution and refined to an R work of 9.1% and an R free of 11.7%. Comparisons with plant thaumatin revealed the electron density of recombinant thaumatin I to be significantly improved, especially around Asn46 and Ser63.
In this study, the catalytic subunit of E. coli AHAS II was cocrystallized with its cofactors Mg2+, FAD and ThDP using the sitting-drop vapour-diffusion method and the crystals diffracted to 2.80 Å resolution.
The P3 dimerization domain of CheA from E. coli has been crystallized (space group P1, unit-cell parameters a = 59.271, b = 67.674, c = 82.815 Å, α = 77.568, β = 86.073, γ = 64.436°). Diffraction data to 2.80 Å resolution have been collected using synchrotron radiation.
A recombinant form of geraniol dehydrogenase from Backhousia citriodora has been overexpressed in Escherichia coli and purified and crystallized by the sitting-drop method using polyethylene glycol 3350 as a precipitant.
The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of phosphoglycerate kinase from S. aureus MRSA252 is reported.
Catechol oxidase from A. oryzae was crystallized by the hanging-drop vapour-diffusion method.
S. Typhimurium CueP has been crystallized. Native data were collected to 2.5 Å resolution.
Factor H-binding protein B from T. denticola was expressed, purified and crystallized. A native data set was collected to 1.8 Å resolution.
Crystals of argininosuccinate lyase from S. mutans were obtained and X-ray data were collected to 2.5 Å resolution in space group R3.
Crystals of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA were obtained and X-ray diffraction data were collected to 1.70 and 3.51 Å resolution, respectively.
Recombinant glucuronic acid dehydrogenase from the halophilic bacterium Chromohalobacter salexigens has been crystallized and X-ray diffraction data collected to a maximum resolution of 2.1 Å.
The Cu-containing nitrite reductase from G. kaustophilus has been overexpressed, purified and crystallized in space group R3. The crystals diffracted to 1.3 Å resolution.
The PH domain of human kindlin-2 was expressed, purified and crystallized. A complete X-ray diffraction data set was obtained at 2.8 Å resolution.
A galactose specific lectin was purified from the seeds of a tropical plant, Spatholobus parviflorus. Its X-ray crystallographic structure was solved by the molecular replacement method.
Recombinant BlaKr has been cocrystallized with kanamycin. A complete data set has been collected to 1.67 Å resolution using synchrotron radiation.
In this study, H. pylori arginase was purified and crystallized in complex with Mn2+ and a diffraction data set was collected to 2.2 Å resolution.
The crystallization and preliminary X-ray crystallographic analysis of the glpX-encoded class II fructose-1,6-bisphosphatase from M. tuberculosis in the apo form is reported.
The purification, characterization and crystallization of a trypsin inhibitor protein isolated from chickpea seeds are reported.
The L. monocytogenes Ca2+-ATPase LMCA1 was crystallized in a Ca2+-free E2–AlF4 − form. A complete data set extending to 4.3 Å resolution was collected and a molecular-replacement solution was obtained using sarcoplasmic reticulum Ca2+-ATPase as a search model.
The cloning, expression, purification, crystallization and preliminary X-ray analysis of a ferric binding protein encoded by T. thermophilus HB8 in apo and iron-bound holo states are presented. Four different crystal forms were obtained.
An O-methyltransferase from the ubiquinone-biosynthesis pathway in Escherichia coli, UbiG, with an N-terminal hexahistidine tag has been expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 2.00 Å resolution.
The eukaryotic translation initiation factor eIF5BΔN and the eIF5BΔN–eIF1AΔN complex from S. cerevisiae were crystallized. The crystals diffracted to maximum resolutions of 2.45 and 3.3 Å, respectively.