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%.