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

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|66|1|48-50

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.66, Iss.1, 2010-01, pp. : 48-50

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Abstract

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%.

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