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The crystal structure of phytase from Debaryomyces castellii has been determined at 2.3 Å resolution.
The crystal structure of the second PDZ domain from human zonula occludens 2 has been determined at 1.75 Å resolution.
The crystal structure of A. faecalis d-3-hydroxybutyrate dehydrogenase prepared in the presence of d-3-hydroxybutyrate and NAD+ reveals the substrate/product-binding geometry as the first example which suggests that the catalytic reaction occurs by shuttle movements of a hydrogen negative ion from the substrate to NAD+ and from NADH to the product.
A Fab fragment of a monoclonal anti-parathyroid hormone-related protein antibody was prepared and its complex with parathyroid hormone-related protein was crystallized. X-ray diffraction data were collected to 2.0 Å resolution.
All organisms examined to date possess a dUTPase that performs the important function of efficiently hydrolyzing dUTP to dUMP in order to prevent the incorporation of dUTP into DNA. Three putative dUTPases from Gram-positive bacteria have been studied in this work.
A 34 kDa chitinase from tamarind (T. indica) seeds was purified, crystallized and characterized using X-ray diffraction.
The multidomain cytoplasmic portion of the histidine protein kinase from an essential two-component signal transduction system has been crystallized and X-ray data have been collected to 2.8 Å resolution.
The crystallization of DNA gyrase B C-terminal domain is described.
A novel haloalkane dehalogenase DbeA from B. elkani USDA94 and its mutant variant DbeA1 were crystallized and diffraction data were collected to 2.2 Å resolution.
Fragaceatoxin C, a newly characterized actinoporin from A. fragacea, has been crystallized. Diffraction data were collected to 1.8 Å resolution.
The SH3 domain of human AHI1 has been cloned and expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and was crystallized using the sitting-drop vapour-diffusion method at 293 K.
A 2.4 Å resolution data set was collected from a crystal of CYP219A1. This is the first protein of a new P450 family from the oligotrophic organism N. aromaticivorans which can oxidize steroids and bind sesquiterpenoids.
Recombinant ATP-dependent DNA ligase from the archaeon Thermococcus sp. 1519 was overexpressed, purified and used to produce crystals that diffracted to 3.09 Å resolution.
The purification, crystallization and preliminary X-ray diffraction studies of vitamin D3 hydroxylase isolated from P. autotrophica are reported.
The haem oxygenase from H. pylori (HugZ) was overexpressed, purified, reconstituted with haem and crystallized. Selenomethionine-derivatized crystals diffracted X-rays to 1.8 Å resolution.
By introducing surface mutations, the crystal quality of a β-lactamase, Toho-1, was drastically improved. The resultant crystals showed no tendency towards merohedral twinning and diffracted to 0.97 Å resolution.
The subtilisin-like serine protease carnein was isolated from the latex of the plant I. carnea, purified and crystallized by the hanging-drop vapour-diffusion method. A diffraction data set was collected to 2.0 Å resolution in-house from a single crystal at 110 K.
A chitinase from the nematophagous fungus C. rosea was overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 1.8 Å resolution.
The human seminal plasma protein PSP94 has been purified from human seminal plasma and crystallized.
Crystallization of SMU.412c protein from the caries pathogen Streptococcus mutans can easily appear in the condition 2.8 M sodium acetate pH 7.0 and its crystal belongs to space group P41212.
Crystals of AKR1B14 were grown from buffered polyethylene glycol solutions and diffracted to 1.86 Å resolution.
The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of triosephosphate isomerase from MRSA252 is reported.
ShuA from S. dysenteriae was crystallized in several crystallization conditions containing detergents. Adding heavy atoms during crystallization strongly improved the crystal quality and the resolution limits. Diffraction data were collected at an energy remote from the Pb M absorption edges.
Perdeuterated type III antifreeze protein has been expressed, purified and crystallized. Preliminary neutron data collection showed diffraction to 1.85 Å resolution from a 0.13 mm3 crystal.
YvoA from B. subtilis, a member of the poorly understood HutC family of bacterial transcription factors, has been recombinantly produced, characterized as a homodimer in solution and crystallized in space group C2.
The d-2-hydroxyacid dehydrogenase from Haloferax mediterranei has been crystallized in two different forms. Diffraction data have been collected to 1.9 Å resolution for the non-productive ternary complex of the enzyme and to 2.7 Å for the selenomethionyl derivative.
The crystallization of xylose reductase from C. tropicalis is reported.
The chicken classical MHC class I antigen YF1*7.1 was crystallized together with β2-microglobulin but without a peptide ligand. Crystals diffracted synchrotron radiation to 1.32 Å and belonged to the monoclinic space group P21.
NtdA was crystallized using the microbatch method. The crystals diffracted to beyond 2.3 Å resolution using synchrotron radiation.