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The first crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) obtained at a neutral pH. LmPYK was co-crystallized with the small molecule 1,3,6,8-pyrenetetrasulfonic acid, which provides a helpful intermolecular bridge between macromolecules.
The structure of DinB from G. stearothermophilus is described and compared with a number of recently reported structures of this unusual fold. Structural similarities are revealed that unite several distant protein families.
A specific Lys–Arg cross-link is observed in trimeric barnase crystals.
The X-ray structure of the anti-IL-23 antibody CNTO4088 reveals an unusual conformation of CDR L1 despite the fact that the residues in key positions fit the pattern of the canonical structure.
The crystal structure of the G170R mutant form of human alanine:glyoxylate aminotransferase has been determined at 2.6 Å resolution. This mutation is associated with enzyme mistargeting in the hereditary kidney-stone disease primary hyperoxaluria type 1.
The structure of a triclinic crystal form of 4-diphosphocytidyl-2C-methyl-d-erythritol kinase has been determined. Comparisons with a previously reported monoclinic crystal form raise questions about our knowledge of the quaternary structure of this enzyme.
Crystal structures of ModA from M. acetivorans in the apo and ligand-bound conformations confirm domain rotation upon ligand binding.
The structure of nitric oxide-treated bovine heart cytochrome c oxidase (CcO) in the fully reduced state was determined at 50 K under light illumination.
The crystal structure of a fully active laccase from Trametes sp. AH28-2 is reported.
Crystals of insulin have been grown from a solution containing insulin and polysialic acid and the three-dimensional structure of insulin in these crystals has been solved at 1.6 Å resolution.
oxyHbII crystals have been grown at pH 4, 5, 8 and 9 by capillary counterdiffusion technique by a two-step protocol: (i) mini screen (searching step) and (ii) pH screen (optimization step).
Crystals of B. cepacia IST408 UDP-glucose dehydrogenase (EC 220.127.116.11) were obtained in space group P212121 and diffracted to 2.09 Å resolution.
The MaoC-like dehydratase from P. capsici was cloned, expressed and purified to homogeneity. Crystals were obtained that diffracted to 1.93 Å resolution.
Cyanide-insensitive alternative oxidase from T. brucei brucei has been purified and crystallized for X-ray structure analysis.
A novel diadenosine 5′,5′′′-P 1,P 4-tetraphosphate phosphorylase from M. tuberculosis H37Rv has been crystallized. The crystal belonged to space group C2 and diffracted X-rays to 1.9 Å resolution.
A thermostable manganese(II)-dependent 2,3-dihydroxybiphenyl-1,2-dioxygenase derived from Bacillus sp. JF8 was crystallized in two forms using the sitting-drop vapour-diffusion method. Both crystals diffracted to approximately 1.3 Å resolution.
Here, the expression, purification, crystallization and preliminary crystallographic analysis of SP0987 from Streptococcus pneumoniae TIGR4 are reported.
The subtilisin-like proteases AprV2 and BprV from virulent strains and AprB2 and BprB from benign strains of D. nodosus have been crystallized and X-ray diffraction data have been collected to 2.0, 2.0, 1.7 and 1.8 Å resolution, respectively.
Community-acquired respiratory distress syndrome toxin (CARDS TX) from M. pneumoniae was cloned, expressed, purified and crystallized. A diffraction data set from a native CARDS TX crystal was obtained at 2.2 Å resolution.
β-Galactosidase from K. lactis has been expressed in S. cerevisiae, purified by affinity chromatography and crystallized in its native form.
Ferredoxin-NADP+ oxidoreductase from B. subtilis has been crystallized by the sitting-drop vapour-diffusion method. Diffraction data were collected to 1.8 Å resolution.
Glycerol kinase from human African trypanosomes has been purified and crystallized for X-ray structure analysis.
An exo-β-d-glucosaminidase from T. reesei (Gls93) has been crystallized by the hanging-drop vapour-diffusion method. Diffraction data have been collected using synchrotron radiation.
Mouse S-adenosyl-l-homocysteine hydrolase has been crystallized in the presence of the reaction product adenosine. Diffraction data to 1.55 Å resolution were collected using synchrotron radiation.
Diffraction-quality crystals of A. fulgidus neelaredoxin have been produced. The expression, purification, crystallization and X-ray crystallographic analysis of A. fulgidus neelaredoxin are reported.
Recombinant rice Os4BGlu12 β-glucosidase purified from E. coli was crystallized with and without 2,4-dinitrophenyl-2-deoxy-2-fluoro-β-d-glucopyranoside.
The full-length subunit E of the ATP synthase from P. horikoshii OT3 was cloned, overexpressed, purified and crystallized. The crystals belonged to space group I4 and diffracted to 3.3 Å resolution using synchrotron radiation.
A multimodular heterotrimeric complex encompassing a trimodular C-terminal fragment of the cellulosomal scaffoldin CipA from C. thermocellum bound to the type II cohesin module of SdbA and the type I dockerin module of CelD has been crystallized by the hanging-drop vapour-diffusion method and initial X-ray diffraction data analysis has been conducted.
1-Deoxy-d-xylulose 5-phosphate reductoisomerase from P. falciparum has been crystallized in the presence of NADPH. Diffraction data to 1.85 Å resolution have been collected using synchrotron radiation.
Phosphoglucose isomerase from P. falciparum has been crystallized. Diffraction data to 1.8 Å resolution have been collected using synchrotron radiation.
The focB gene from E. coli was cloned and the protein was expressed and purified. The protein is oligomeric, most likely in the form of dimers. NMR analysis showed that line broadening significantly increases at temperatures below 293 K, presumably owing to increased conformational exchange or oligomerization. Crystals were obtained at room temperature and diffracted to better than 2.0 Å...
The catalytic subunits of the human pyruvate dehydrogenase phosphatase isoforms 1 and 2 have been purified and crystallized. The crystals of PDP1c and PDP2c diffracted to 2.45 and 2.0 Å resolution, respectively.
Preliminary crystallographic studies of recombinant cellobiose phosphorylase from Cellulomonas uda in complex with reaction substrates and products have led to high-quality diffraction data at high resolution, thus enabling structural studies to dissect the structural and mechanistic determinants of disaccharide phosphorylase activity.
Microcrystals of HpaB were formed while isolating integral membrane respiratory complexes from Thermus thermophilus. Further purification of the enzyme was achieved by repetitive crystallization. Subsequently, well shaped single crystals of the native enzyme that diffracted to 1.82 Å resolution were grown in sitting drops.
Mouse peroxiredoxin II was crystallized in an orthorhombic space group and native X-ray diffraction data were collected.
Plant plasma-membrane Ca2+-ATPase is regulated via binding of calmodulin to its autoinhibitory N-terminal domain. In this study, the expression, purification, crystallization and preliminary X-ray diffraction analysis of this protein complex from A. thaliana are reported.
The effectiveness of using ultraviolet microscopes to illuminate protein crystals in high throughput screens is evaluated.