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Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus strain Mu50.

ABSTRACT: DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological form of bacterial DNA. In this study, the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus Mu50 strain was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.80?Å resolution using a synchrotron-radiation source. The crystal belonged to space group P2(1), with unit-cell parameters a = 37.28, b = 80.19, c = 50.22?Å, ? = 110.64°. The asymmetric unit contained one molecule, with a corresponding V(M) of 2.02?Å(3)?Da(-1) and a solvent content of 39.2%.

SUBMITTER: Kim TO

PROVIDER: S-EPMC3034627 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus strain Mu50.

Kim Tae-O TO Jung Ha Yun HY Lee Soo Young SY Im Dong-Won DW Shin Whanchul W Heo Yong-Seok YS

Acta crystallographica. Section F, Structural biology and crystallization communications 20110127 Pt 2

DNA gyrase is a type II topoisomerase that is essential for chromosome segregation and cell division owing to its ability to modify the topological form of bacterial DNA. In this study, the C-terminal domain of the GyrA subunit of DNA gyrase from Staphylococcus aureus Mu50 strain was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.80 Å resolution using a synchrotron-radiation source. The crystal belonged to space group P2(1), with unit-cell para ...[more]

PMID: 21301105

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