Open AccessPurification, crystallization and preliminary X‐ray analysis of SGR6054, a Streptomyces homologue of the mycobacterial integration host factor mIHF
Author(s) -
Nomoto Ryohei,
Tezuka Takeaki,
Miyazono Kenichi,
Tanokura Masaru,
Horinouchi Sueharu,
Ohnishi Yasuo
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112030631
Subject(s) - mycobacterium smegmatis , streptomyces coelicolor , streptomyces griseus , escherichia coli , biology , microbiology and biotechnology , crystallization , mycobacterium , dna , streptomyces , bacteria , mycobacterium tuberculosis , crystallography , chemistry , gene , biochemistry , genetics , tuberculosis , medicine , pathology , organic chemistry
The mycobacterial integration host factor (mIHF) is a small nonspecific DNA‐binding protein that is essential for the growth of Mycobacterium smegmatis . mIHF homologues are widely distributed among Actinobacteria, and a Streptomyces homologue of mIHF is involved in control of sporulation and antibiotic production in S. coelicolor A3(2). Despite their important biological functions, a structure of mIHF or its homologues has not been elucidated to date. Here, the S. griseus mIHF homologue (SGR6054) was expressed and purified from Escherichia coli and crystallized in the presence of a 16‐mer duplex DNA by the sitting‐drop vapour‐diffusion method. The plate‐shaped crystal belonged to space group C 2, with unit‐cell parameters a = 88.53, b = 69.35, c = 77.71 Å, β = 96.63°, and diffracted X‐rays to 2.22 Å resolution.