title: 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, β = 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%.
authors.affiliation: Department of Chemistry, Konkuk University, Seoul, Republic of Korea.
authors.forename: Tae-O
authors.initials: TO
authors.lastname: Kim
authors.forename: Ha Yun
authors.initials: HY
authors.lastname: Jung
authors.forename: Soo Young
authors.initials: SY
authors.lastname: Lee
authors.forename: Dong-Won
authors.initials: DW
authors.lastname: Im
authors.forename: Whanchul
authors.initials: W
authors.lastname: Shin
authors.forename: Yong-Seok
authors.initials: YS
authors.lastname: Heo
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D027081:DNA Gyrase / Q000737:chemistry* / Q000302:isolation & purification; D004250:DNA Topoisomerases, Type II / Q000302:isolation & purification; D004926:Escherichia coli / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D013211:Staphylococcus aureus / Q000737:chemistry*; D017356:Synchrotrons
chemical_list: D001426:Bacterial Proteins; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II