Preliminary X-ray crystallographic analysis of the breakage-reunion domain of the GyrA subunit of DNA gyrase from Colwellia psychrerythraea strain 34H.
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 A resolution using a synchrotron-radiation source. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 98.98, b = 101.56, c = 141.83 A. The asymmetric unit contained two molecules, with a corresponding V(M) of 3.18 A(3) Da(-1) and a solvent content of 59.9%.
Jung
Ha Yun
HY
Department of Chemistry, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.
Kim
Kyung Ha
KH
Hyoung
Ji Hye
JH
Han
Mi Ra
MR
Kim
Hyun Kyoung
HK
Lee
Ki Jeung
KJ
Kim
Yangmee
Y
Kim
Hak Jun
HJ
Heo
Yong Seok
YS
D034241:Alteromonadaceae / Q000201:enzymology*; D018360:Crystallography, X-Ray; D027081:DNA Gyrase / Q000737:chemistry*
D027081:DNA Gyrase
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