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Crystallization and preliminary X‐ray crystallographic analysis of DNA gyrase GyrB subunit from Xanthomonas oryzae pv. oryzae
Author(s) -
Jung Ha Yun,
Lee Ki Jeung,
Kim Kyung Ha,
Hyoung Ji Hye,
Han Mi Ra,
Kim Hyun Kyoung,
Kang LinWoo,
Ahn YehJin,
Heo YongSeok
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109047721
Subject(s) - dna gyrase , xanthomonas oryzae , xanthomonas oryzae pv. oryzae , dna , protein subunit , escherichia coli , crystallography , chromosome , crystallization , bacterial blight , biology , microbiology and biotechnology , chemistry , genetics , bacteria , gene , organic chemistry
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 I 4 1 , 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 Å 3  Da −1 and a solvent content of 50.2%.

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