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crystallization communications
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 VM of 2.57 Å3 Da-1 and a solvent content of 50.2%.