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


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 A resolution using a synchrotron-radiation source. The crystal belonged to space group I4(1), with unit-cell parameters a = b = 110.27, c = 70.75 A. The asymmetric unit contained one molecule, with a V(M) of 2.57 A(3) Da(-1) and a solvent content of 50.2%.

SUBMITTER: Jung HY 

PROVIDER: S-EPMC2805535 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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

Jung Ha Yun HY   Lee Ki Jeung KJ   Kim Kyung Ha KH   Hyoung Ji Hye JH   Han Mi Ra MR   Kim Hyun Kyoung HK   Kang Lin-Woo LW   Ahn Yeh-Jin YJ   Heo Yong-Seok YS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20091225 Pt 1


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 A resolution using a synchrotron-radiation source. The crystal belonged to space group I4(1), with unit-cell param  ...[more]

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