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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):612-4. doi: 10.1107/S1744309109016649. Epub 2009 May 22.

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

Author information

1
Department of Chemistry, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.

Abstract

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%.

PMID:
19478444
PMCID:
PMC2688423
DOI:
10.1107/S1744309109016649
[Indexed for MEDLINE]
Free PMC Article

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