Crystallization and preliminary X-ray crystallographic analysis of DNA gyrase GyrB subunit from Xanthomonas oryzae pv. oryzae

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 fragment of the GyrB subunit of DNA gyrase from Xanthomonas oryzae pv. oryzae was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.10 Å resolution using a synchrotron-radiation source. The crystal belonged to space group I4₁, with unit-cell parameters a = b = 110.27, c = 70.75 Å. The asymmetric unit contained one molecule, with a V_M of 2.57 Å³ Da^-1 and a solvent content of 50.2%.