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The X-ray crystal structure of the Trx-fold domain of hPDCL2 was solved at 2.70 Å resolution and resembled the Trx-fold domain of rat phosducin.
The crystal structure of the ligand-binding domain of a receptor tyrosine kinase EphB2, an important mediator of cell-cell communication, has been determined at a resolution of 2 Å. The structure confirms the induced-fit mechanism for the binding of ligands to EphB receptors.
The crystal structure of human protein kinase CK2α2 with a potent indazole-derivative inhibitor has been determined at 3.2 Å resolution.
X-ray structures of ferric cytochrome P450cam partially complexed with the substrate (+)-camphor to two different extents were determined at 1.30–1.35 Å resolution, revealing the protein structures of the substrate-free and substrate-bound forms.
The crystal structure of iron superoxide dismutase from the cold-adapted organism A. salmonicida has been determined at a resolution of 1.7 Å.
The crystallization and X-ray analysis of recombinant human cytosolic phenylalanyl-tRNA synthetase (hcPheRS) are reported. Diffraction data were collected to 3.3 Å resolution and the hcPheRS structure was determined by the molecular-replacement method using phase information derived from multiwavelength anomalous dispersion data.
Various E. coli tRNAArg acceptor-stem microhelix isoacceptors have been crystallized and investigated by high-resolution X-ray diffraction analysis.
The human cytokine IL-22 has been crystallized in complex with its soluble decoy receptor IL-22BP. Diffraction data were collected to 2.75 Å resolution; the crystals belonged to the tetragonal space group P41.
The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 K using the hanging-drop vapour-diffusion method.
The second RRM of Pub1 from S. cerevisiae was overexpressed, purified and crystallized. Diffraction data were collected to 1.69 Å resolution.
Degradation-free crystalization of thrombin-digested recombinant His-tagged PsbP protein of photosystem II from Spinacia oleracea resulting in crystals diffracting to 2.06 Å.
The hexameric Cu-containing nitrite reductase and its electron-donor protein pseudoazurin have been cocrystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 3.3 Å resolution using a synchrotron-radiation source.
Crystallization of pigeon haemoglobin at low pH (5.5) and high ionic concentration (1 M) using the hanging-drop vapour-diffusion method is reported.
The soluble domain of a putative copper-containing nitrite reductase from P. acnes has been overexpressed, purified and crystallized. The crystal belonged to space group P213 and diffracted to 2.4 Å resolution.
Preliminary X-ray analysis of crystals of the bacterial microcompartment shell protein Eut-L from Escherichia coli is reported.
The catalytic module of a family 101 glycoside hydrolase from S. pneumoniae was cloned, recombinantly produced and crystallized.
Two C-terminally truncated variants of the small subunit of isopropylmalate isomerase from M. tuberculosis have been cloned, expressed, purified, crystallized and examined by X-ray diffraction.
Crystallization of CcCel6C was carried out by the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.6 Å resolution from the crystal.
The C-terminal domain protein of the PB2 subunit of influenza A virus RNA-dependent RNA polymerase was expressed and crystallized and diffraction data were obtained from the crystals.
Crystals of the 45.1 kDa functional form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from B. subtilis diffracted to 2.30 Å resolution.
A complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. Crystals of this intramolecular complex diffracted to 2.16 Å resolution.
The cloning, overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the transcriptional repressor SirR (staphylococcal iron regulator) from M. tuberculosis are reported.
The chromophore-binding domain of cyanobacteriochrome AnPixJ was overproduced in E. coli, purified and crystallized in its red-absorbing form. Diffraction data were then collected to a resolution of 1.8 Å.
Native and selenomethionine-labeled crystals of Ebola VP35 interferon inhibitory domain were obtained by the hanging-drop vapor-diffusion method.
An alkaline alanine racemase from alkaliphilic B. pseudofirmus OF4 was expressed in E. coli and purified. Crystallization and preliminarily X-ray crystallographic analysis were performed for the recombinant enzyme.
The yeast N-acetyltransferase that N-acetylates l-azetidine-2-carboxylic acid has been crystallized. Native data were collected to 1.9 Å resolution from a substrate-soaked crystal.
Rv1653, an ornithine acetyltransferase from M. tuberculosis, has been crystallized and diffraction data have been collected to 1.7 Å resolution.
Crystals of adeno-associated virus serotype 3b, a human DNA virus with promise as a vector for gene therapy, have been grown, diffract X-rays to ~2.6 Å resolution and are suitable for structure determination in spite of twinning.
Preliminary neutron crystallographic data from the serine protease proteinase K have been recorded using the LADI-III diffractometer at the Institut Laue–Langevin. The results illustrate the feasibility of a full neutron structural analysis aimed at further understanding the catalytic mechanism of proteinase K.
Dihydrodipicolinate synthase (DHDPS) catalyses an important step in lysine biosynthesis. Here, the expression, purification, crystallization and preliminary diffraction analysis to 2.15 Å resolution of DHDPS from B. anthracis soaked with the substrate pyruvate are reported.