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Purification, crystallization and preliminary X-ray analysis of SGR6054, a Streptomyces homologue of the mycobacterial integration host factor mIHF

Abstract

A Streptomyces homologue of the mycobacterial integration host factor mIHF was heterologously produced, purified and crystallized in the presence of a 16-mer duplex DNA by the sitting-drop vapour-diffusion method. The best crystal diffracted X-rays to 2.22 Å resolution and belonged to space group C2. 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 C2, 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.
Authors:
Nomoto, Ryohei; Tezuka, Takeaki; Miyazono, Ken-ichi; Tanokura, Masaru; Horinouchi, Sueharu; Ohnishi, Yasuo [1] 
  1. Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657 (Japan)
Publication Date:
Aug 31, 2012
Product Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 68; Journal Issue: Pt 9; Other Information: PMCID: PMC3433204; PMID: 22949201; PUBLISHER-ID: hc5149; OAI: oai:pubmedcentral.nih.gov:3433204; Copyright (c) International Union of Crystallography 2012; Country of input: International Atomic Energy Agency (IAEA)
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; DNA; ESCHERICHIA COLI; PLATES; RESOLUTION; SPACE GROUPS
OSTI ID:
22374694
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 1744-3091; CODEN: ACSFCL; Other: PII: S1744309112030631; TRN: GB15$1638080076
Availability:
Available from http://dx.doi.org/10.1107/S1744309112030631; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3433204
Submitting Site:
INIS
Size:
page(s) 1085-1088
Announcement Date:
Aug 11, 2015

Citation Formats

Nomoto, Ryohei, Tezuka, Takeaki, Miyazono, Ken-ichi, Tanokura, Masaru, Horinouchi, Sueharu, and Ohnishi, Yasuo. Purification, crystallization and preliminary X-ray analysis of SGR6054, a Streptomyces homologue of the mycobacterial integration host factor mIHF. United Kingdom: N. p., 2012. Web. doi:10.1107/S1744309112030631.
Nomoto, Ryohei, Tezuka, Takeaki, Miyazono, Ken-ichi, Tanokura, Masaru, Horinouchi, Sueharu, & Ohnishi, Yasuo. Purification, crystallization and preliminary X-ray analysis of SGR6054, a Streptomyces homologue of the mycobacterial integration host factor mIHF. United Kingdom. doi:10.1107/S1744309112030631.
Nomoto, Ryohei, Tezuka, Takeaki, Miyazono, Ken-ichi, Tanokura, Masaru, Horinouchi, Sueharu, and Ohnishi, Yasuo. 2012. "Purification, crystallization and preliminary X-ray analysis of SGR6054, a Streptomyces homologue of the mycobacterial integration host factor mIHF." United Kingdom. doi:10.1107/S1744309112030631. https://www.osti.gov/servlets/purl/10.1107/S1744309112030631.
@misc{etde_22374694,
title = {Purification, crystallization and preliminary X-ray analysis of SGR6054, a Streptomyces homologue of the mycobacterial integration host factor mIHF}
author = {Nomoto, Ryohei, Tezuka, Takeaki, Miyazono, Ken-ichi, Tanokura, Masaru, Horinouchi, Sueharu, and Ohnishi, Yasuo}
abstractNote = {A Streptomyces homologue of the mycobacterial integration host factor mIHF was heterologously produced, purified and crystallized in the presence of a 16-mer duplex DNA by the sitting-drop vapour-diffusion method. The best crystal diffracted X-rays to 2.22 Å resolution and belonged to space group C2. 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 C2, 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.}
doi = {10.1107/S1744309112030631}
journal = {Acta Crystallographica. Section F}
issue = {Pt 9}
volume = {68}
journal type = {AC}
place = {United Kingdom}
year = {2012}
month = {Aug}
}