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Three crystal structures of the molybdenum-cofactor biosynthesis protein MogA from two highly thermophilic organisms have been determined at high resolution. Comparative analyses revealed the residues involved in oligomerization. In addition, molecular-dynamics and docking studies suggested the binding affinities of several small molecules towards MogA and homologous proteins.
The crystal structure of SEp22, a DNA-binding protein from starved cells from S. enterica subsp. enterica serovar Enteritidis, was determined in two forms: the native state at 1.25 Å resolution and an iron-soaked form at 1.30 Å resolution.
The structure of the C-terminal domain of the S. mutans surface adhesin SpaP has been determined to 2.2 Å resolution.
The structure of the small laccase from S. coelicolor is reported at improved resolution and in a different space group. The soaked ligand is bound between laccase molecules.
The structure of L. donovani pteridine reductase has been targeted to assist in a program of structure-based inhibitor research. Crystals that diffracted to 2.5 Å resolution were obtained and the structure has been solved. Unfortunately, the active site is disordered and this crystal form is unsuitable for use in characterizing enzyme–ligand interactions.
H. sapiens quinolinate phosphoribosyltransferase has been expressed, purified and crystallized. A diffraction data set has been collected and processed at 2.8 Å resolution.
Crystals of native intimin and its N916Y mutant from enterohaemorrhagic E. coli O157:H7 diffracted to 2.8 and 2.6 Å resolution, respectively.
Bacterial blight, an infectious disease caused by X. oryzae pv. oryzae (Xoo), causes huge rice-production losses in most rice-cultivating countries. The co-chaperonin of Xoo, XoGroES, an important protein for protein folding, was cloned from Xoo, purified and crystallized for atomic resolution structure determination.
The human G3BP1 NTF2-like domain was crystallized. Diffraction data were collected to 3.6 Å resolution.
Crystals of the thiaminase type II from S. aureus are orthorhombic, belonging to space group P212121 with unit-cell parameters a = 103.5, b = 104.1, c = 109.6 Å, and diffracted to 2.6 Å resolution.
Human α-thrombin was crystallized in complex with specific peptide inhibitors of general sequence d-Phe-Pro-d-Arg-P1′-CONH2. The crystals belonged to the orthorhombic space group P212121 and diffracted to beyond 1.3 Å resolution.
Biphenyl 2,3-dioxygenase from B. xenovorans LB400 and its variants BPDOP4 and BPDORR41 were crystallized using agarose gel and the crystals were characterized using X-ray diffraction.
The vWA domain of human anthrax toxin receptor 1 was overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 1.8 Å resolution.
α-Glucuronidase from S. pristinaespiralis was crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group R3 and diffracted to a resolution of 1.9 Å.
The cloning, expression, purification, crystallization and preliminary X-ray analysis of wild-type and of an active-site mutant of C. jejuni glyceraldehyde-3-phosphate dehydrogenase is reported.
SMU.1108c, a putative uncharacterized protein from S. mutans, was crystallized and X-ray diffraction data were collected to a resolution of 2.2 Å.
The purification, crystallization and preliminary X-ray diffraction analysis of RNase HIII from S. aureus is presented. Crystals that diffracted to 2.6 Å resolution in space group P212121 were only obtained after removal of the hexahistidine tag.
ESX-1 secreted protein regulator (EspR, Rv3849) from M. tuberculosis has been purified and crystallized, and diffracted to 3.2 Å resolution at wavelength 0.97625 Å.
Crystallization of basic 7S globulin from soybean is presented.
An apo form of human arginase I which is suitable for soaking experiments has been crystallized.
In order to investigate its structure and function, the NmrA-like domain-containing DDB_G0286605 protein from D. discoideum was expressed, purified and crystallized. X-ray diffraction analysis is reported to a resolution of 1.64 Å.
In order to investigate its structure and function, the NmrA-like short-chain dehydrogenase/reductase-type DDB_G0291732 protein from D. discoideum was expressed, purified and crystallized. X-ray diffraction analysis is reported to a resolution of 1.65 Å.
Isopentenyl diphosphate isomerase from M. jannaschii has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.08 Å resolution.
The small terminase subunit of bacteriophage P22 was overexpressed in E. coli, purified under native conditions and crystallized as a nonamer. High-quality diffraction data were collected to 1.75 Å resolution using synchrotron radiation.
A β-glucosidase A (BglA) from the thermophile Halothermothrix orenii has been cloned, purified and crystallized in an orthorhombic space group. X-ray diffraction data have been collected to 3.5 Å resolution, and the structure was solved by molecular replacement, revealing the presence of two molecules in the asymmetric unit.
The crystallization of E. coli maltoporin in a new crystal form that diffracts to high resolution is reported.
Wild-type and a kinase-dead mutant of the C-terminal serine/threonine kinase domain of CTR1 from A. thaliana were expressed and crystallized. The crystals belonged to space groups P41212 and P42212, respectively.
PpAzoR, an FMN-dependent NADPH azoreductase from Pseudomonas putida MET94, has been crystallized using the sitting-drop vapour-diffusion technique.
Glycosylated recombinant bifunctional nuclease from tomato has been crystallized and preliminary X-ray diffraction analysis was performed.
LR11/sorLA contains in its extracellular region a large (~700-residue) Vps10p domain that is implicated in its intracellular protein-trafficking function. Here, the expression, purification, crystallization and preliminary crystallographic characterization of this domain are described.
NifH2, a homologue of nitrogenase reductase from Methanocaldococcus jannaschii was cloned, overexpressed, purified and crystallized. X-ray diffraction data were collected to 2.85 Å resolution and the crystals belonged to space group P2.
The recombinant glycosyltransferase ElaGT from the elaiophylin-producing marine Streptomyces sp. SCSIO 01934 has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.9 Å resolution.
A variant of the diaminopimelate/lysine pathway has recently been defined following the discovery of the enzyme l,l-diaminopimelate aminotransferase (DapL). The cloning of the cDNA, recombinant expression, purification and preliminary diffraction analysis of DapL from the alga C. reinhardtii are presented.
The KaiC-like protein PH0187 from the hyperthermophilic archaeon P. horikoshii OT3 was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal of PH0187 diffracted X-rays to 2.75 Å resolution.
d-Serine dehydratase purified from chicken kidney was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.09 Å resolution.
The crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-d-xylanase is described. The crystals diffracted to 2.7 Å resolution.
The seryl-tRNA synthetase from C. albicans was crystallized by the sitting-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belonged to the hexagonal space group P6122 and diffraction data were collected to 2.0 Å resolution at a synchrotron source.
Limited proteolysis of a monomeric fraction of Tellina virus 1 VP4 protease leads to crystals that diffract to beyond 2.1 Å resolution.
Crystals of the lytic transglycosylase MltE from E. coli were grown using the microbatch method and diffracted to a resolution of 2.1 Å.
In this study, the region 115–362 of the resuscitation-promoting factor RpfB was cloned, expressed and crystallized. This region includes the C-terminal catalytic domain, the G5 domain and one of the three DUF348 domains, which are of previously unknown structure and function.
The genome sequence of mimivirus, the largest known double-stranded DNA virus, encodes a putative protease: the R355 gene product. Its expression in E. coli, its crystallization and the preliminary phasing of a MAD data set using the selenium signal present in a crystal of recombinant selenomethionine-substituted protein are reported.
Notes for authors.