Crystallization and X-ray diffraction data collection of topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae.

Topoisomerase IV is involved in topological changes in the bacterial genome using the free energy from ATP hydrolysis. Its functions are the decatenation of daughter chromosomes following replication by DNA relaxation and double-strand DNA breakage. In this study, the N-terminal fragment of the topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.15 A resolution using a synchrotron-radiation source. The crystal belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 105.30, c = 133.76 A. The asymmetric unit contains one molecule, with a corresponding V(M) of 4.21 A(3) Da(-1) and a solvent content of 69.6%.