Open AccessCrystallization and X‐ray diffraction data collection of topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae
Author(s) -
Shin Hye Jeong,
Yun Mirim,
Song JuYeon,
Kim Hyun Jeong,
Heo YongSeok
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109016649
Subject(s) - xanthomonas oryzae , topoisomerase , escherichia coli , protein subunit , topoisomerase iv , crystallography , dna , crystallization , xanthomonas oryzae pv. oryzae , chemistry , biology , microbiology and biotechnology , biophysics , dna gyrase , biochemistry , genetics , bacteria , gene , organic chemistry
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 Å resolution using a synchrotron‐radiation source. The crystal belonged to space group P 4 2 2 1 2, with unit‐cell parameters a = b = 105.30, c = 133.76 Å. The asymmetric unit contains one molecule, with a corresponding V M of 4.21 Å 3 Da −1 and a solvent content of 69.6%.