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Title: Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis

Abstract

Preliminary crystallographic data are reported for the third SRP GTPase FlhF from Bacillus subtilis. The Gram-positive bacterium Bacillus subtilis contains three proteins belonging to the signal recognition particle (SRP) type GTPase family. The well characterized signal sequence-binding protein SRP54 and the SRP receptor protein FtsY are universally conserved components of the SRP system of protein transport. The third member, FlhF, has been implicated in the placement and assembly of polar flagella. This article describes the overexpression and preliminary X-ray crystallographic analysis of an FlhF fragment that corresponds to the well characterized GTPase domains in SRP54 and FtsY. Three crystal forms are reported with either GDP or GMPPNP and diffract to a resolution of about 3 Å.

Authors:
; ; ;  [1]
  1. Heidelberg University Biochemistry Centre (BZH), INF 328, 69120 Heidelberg (Germany)
Publication Date:
OSTI Identifier:
22360330
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335006; PMID: 17565194; PUBLISHER-ID: gj5018; OAI: oai:pubmedcentral.nih.gov:2335006; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALS; RECEPTORS; RESOLUTION; SIGNALS

Citation Formats

Bange, Gert, Petzold, Georg, Wild, Klemens, and Sinning, Irmgard, E-mail: irmi.sinning@bzh.uni-heidelberg.de. Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107020180.
Bange, Gert, Petzold, Georg, Wild, Klemens, & Sinning, Irmgard, E-mail: irmi.sinning@bzh.uni-heidelberg.de. Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis. United Kingdom. doi:10.1107/S1744309107020180.
Bange, Gert, Petzold, Georg, Wild, Klemens, and Sinning, Irmgard, E-mail: irmi.sinning@bzh.uni-heidelberg.de. Tue . "Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis". United Kingdom. doi:10.1107/S1744309107020180.
@article{osti_22360330,
title = {Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis},
author = {Bange, Gert and Petzold, Georg and Wild, Klemens and Sinning, Irmgard, E-mail: irmi.sinning@bzh.uni-heidelberg.de},
abstractNote = {Preliminary crystallographic data are reported for the third SRP GTPase FlhF from Bacillus subtilis. The Gram-positive bacterium Bacillus subtilis contains three proteins belonging to the signal recognition particle (SRP) type GTPase family. The well characterized signal sequence-binding protein SRP54 and the SRP receptor protein FtsY are universally conserved components of the SRP system of protein transport. The third member, FlhF, has been implicated in the placement and assembly of polar flagella. This article describes the overexpression and preliminary X-ray crystallographic analysis of an FlhF fragment that corresponds to the well characterized GTPase domains in SRP54 and FtsY. Three crystal forms are reported with either GDP or GMPPNP and diffract to a resolution of about 3 Å.},
doi = {10.1107/S1744309107020180},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}