|Home | About | Journals | Submit | Contact Us | Français|
Re-refinement of three models of human placental alkaline phosphatase resulted in improved models for the protein and led to proper definition of the bound ligands. The PNP molecules found in the new models have consistent interactions at the original peripheral site and an additional peripheral site.
The structures of two new crystal forms of human Cu/Zn superoxide dismutase produced in the eukaryotic expression host L. tarentolae are reported.
The 1.6 Å resolution structure of a fibronectin type III-like module from Clostridium thermocellum (PDB code 3mpc) with two molecules in the asymmetric unit is reported.
The crystal structure of the catalytic core of the primate foamy virus integrase was solved to 2 Å resolution and in several different crystal forms. The effect of divalent cations and of mutations on the structure is discussed.
The molecule of uracil-DNA glycosylase from M. tuberculosis exhibits domain motion on binding to DNA or a proteinaceous inhibitor. The highly conserved DNA-binding region interacts with a citrate ion in the structure.
Structures of hypoxanthine-guanine phosphoribosyltransferase from T. thermophilus HB8 in the unliganded form, in complex with IMP and in complex with GMP are reported at 2.1, 1.9 and 2.2 Å resolution, respectively.
Purified transketolase from L. salivarius has been crystallized using the vapour-diffusion technique.
The tandem tudor domain of Sgf29 from S. cerevisiae has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 1.92 Å resolution.
MnmE from P. aeruginosa was crystallized and X-ray diffraction data were collected to 2.69 Å resolution.
Crystals of SAICAR synthase from S. suis serotype 2 were obtained in the presence of 40 mM aspartic acid substrate; they belonged to space group P2 and diffracted to 2.8 Å resolution.
The E. coli transcription repressor LsrR has been overexpressed, purified and crystallized. Diffraction data were collected to about 3 Å resolution.
In order to investigate its function in transcriptional gene silencing, the highly conserved motif 2 from A. thaliana Morpheus’ molecule 1 protein was expressed, purified and crystallized. X-ray diffraction analysis is reported to a resolution of 3.2 Å.
High level expression of soluble amaranth 11S proglobulin in Escherichia coli and its purification are described. Crystallization of the recombinant protein and crystal data collection are also presented.
The omega-transaminase from V. fluvialis JS17 was crystallized. Crystals were found to belong to the orthorhombic space group P212121, with unit-cell parameters a = 78.43, b = 95.95, c = 122.89 Å. The crystals were obtained at 293 K and diffracted to a resolution of 2.5 Å.
The SET/TAF-Iβ that lacked the first 22 residues of the N-terminus from Homo sapiens was recombinantly expressed in Escherichia coli and crystallized. X-ray diffraction data were collected to 2.7 Å resolution.
In this study, recombinant OmpAC from EHEC was purified and crystallized and a diffraction data set was collected to 2.7 Å resolution.
Crystallization of the ADP-ribosyltransferase HopU1 is reported.
Full-length human Fas apoptosis inhibitory molecule (FAIM) and two truncation constructs have successfully been cloned, expressed and purified in Escherichia coli. FAIM (1–90) was crystallized and diffracted to a resolution of 2.5 Å.
Recombinant L. jensenii enolase has been expressed, purified and crystallized. The crystals diffracted to 3.25 Å resolution.
Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase from B. breve was overexpressed and crystallized. The crystals belonged to the tetragonal space group I422 and diffracted to beyond 1.7 Å resolution.
A chemotaxis response regulator CheY3 from V. cholerae has been cloned, overexpressed, purified and crystallized. The crystals of CheY3 diffracted to 1.86 Å resolution.
Curcuminoid synthase from O. sativa has been overexpressed in E. coli, purified and crystallized. Diffraction data have been collected to a resolution of 2.5 Å.
The putative aldose 1-epimerase YeaD from Escherichia coli was crystallized and diffraction data were collected to a resolution of 1.9 Å.
Tubulin-folding cofactor A from A. thaliana has been crystallized and preliminarily analyzed using X-ray diffraction.
Phosphorylcholine phosphatase from P. aeruginosa has been crystallized. Diffraction data have been collected to 2.7 Å resolution.
The complex between human α-thrombin and a modified thrombin-binding aptamer has been crystallized. Diffraction data were collected to 2.15 Å resolution, the structure was solved by molecular replacement and refinement of the model is in progress.
The crystallization of BMP receptor type IA bound to the neutralizing antibody Fab fragment AbD1556 obtained by phage-display selection is reported.
The effect of laser irradiation on freshly prepared protein drops was explored and found to be a viable tool to induce nucleation. In our experiment, the number of positive crystallization hits during the screening process increased. In some instances the speed of crystal growth, the size of the crystals and the resolution of X-ray diffraction showed a marked improvement after laser exposure. Under...