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Corresponding VM (corresponding + vm)

Distribution by Scientific Domains
Chemistry100%

Selected Abstracts

Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a ,-­ketoacyl carrier protein reductase homologue

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2002
Jin Kuk Yang
A 260-residue protein (FabG3) encoded by the Rv2002 gene of Mycobacterium tuberculosis shows amino-acid sequence similarity to ,-ketoacyl carrier protein (ACP) reductase, FabG. A soluble mutant (I6T/V47M/T69M) was produced by the green fluorescent protein-based directed-evolution method. It was crystallized at 296,K using the hanging-drop vapour-diffusion method. The diffraction quality of the crystal improved significantly after annealing/dehydration. X-ray diffraction data were collected to 1.8,Å resolution using synchrotron radiation. The crystal belongs to the space group P3121 (or P3221), with unit-cell parameters a = b = 70.38, c = 148.93,Å. The asymmetric unit contains two subunits, with a corresponding VM of 1.90,Å3,Da,1 and a solvent content of 35.3%. [source]

Preliminary X-ray crystallographic analysis of the breakage,reunion domain of the GyrA subunit of DNA gyrase from Colwellia psychrerythraea strain 34H

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2010
Ha Yun Jung
DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological forms of bacterial DNA. In this study, the N-terminal breakage,reunion domain of the GyrA subunit of DNA gyrase from Colwellia psychrerythraea 34H was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.60,Å resolution using a synchrotron-radiation source. The crystal belonged to space group P212121, with unit-cell parameters a = 98.98, b = 101.56, c = 141.83,Å. The asymmetric unit contained two molecules, with a corresponding VM of 3.18,Å3,Da,1 and a solvent content of 59.9%. [source]

Crystallization and X-ray diffraction data collection of topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009
Hye Jeong Shin
Topoisomerase IV is involved in topological changes in the bacterial genome using the free energy from ATP hydrolysis. Its functions are the decatenation of daughter chromosomes following replication by DNA relaxation and double-strand DNA breakage. In this study, the N-terminal fragment of the topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.15,Å resolution using a synchrotron-radiation source. The crystal belonged to space group P42212, with unit-cell parameters a = b = 105.30, c = 133.76,Å. The asymmetric unit contains one molecule, with a corresponding VM of 4.21,Å3,Da,1 and a solvent content of 69.6%. [source]

Crystallization and preliminary X-ray crystallographic studies of the ,-class glutathione S -transferase from the Antarctic clam Laternula elliptica

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2008
Eun Hyuk Jang
Glutathione S -transferases are involved in phase II detoxification processes and catalyze the nucleophilic attack of the tripeptide glutathione on a wide range of endobiotic and xenobiotic electrophilic substrates. The ,-class glutathione S -transferase from Laternula elliptica was overexpressed in Escherichia coli, purified and crystallized with two substrates: glutathione and 1-chloro-2,4-dinitrobenzene (CDNB). Diffraction data were collected to 2.20,Å resolution for the glutathione-complex crystals and to 2.00,Å resolution for the CDNB-complex crystals using a synchrotron-radiation source. Both crystals belonged to the C -centred monoclinic space group C2. The unit-cell parameters for the CDNB-complex crystals were a = 89.66, b = 59.27, c = 55.45,Å, , = 124.52°. The asymmetric unit contained one molecule, with a corresponding VM of 2.36,Å3,Da,1 and a solvent content of 47.8%. [source]