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Crystallization and preliminary X-ray analysis of RsbS from Moorella thermo­acetica at 2.5 Å resolution

DOI: 10.1107/S1744309108003849 DOI Help
PMID: 18323607 PMID Help

Authors: Maureen Quin (Newcastle University) , Joseph Newman (Newcastle University) , Susan Firbank (Newcastle University) , Richard J. Lewis (Newcastle University) , Jon Marles-wright (Newcastle University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 (3) , PAGES 196 - 199

State: Published (Approved)
Published: March 2008

Open Access Open Access

Abstract: The thermophilic bacterium Moorella thermoacetica possesses an rsb operon that is related to the genetic locus common to many Gram-positive bacteria that regulates the activity of the stress-responsive sigma factor B. One of the gene products of this operon is RsbS, a single STAS-domain protein that is a component of higher order assemblies in Bacillus subtilis known as `stressosomes'. It is expected that similar complexes are found in M. thermoacetica, but in this instance regulating the biosynthesis of cyclic di-GMP, a ubiquitous secondary messenger. Selenomethionine-labelled MtRsbS protein was crystallized at room temperature using the hanging-drop vapour-diffusion method. Crystals belonging to space group P212121, with unit-cell parameters a = 51.07, b = 60.52, c = 89.28 Å, diffracted to 2.5 Å resolution on beamline I04 of the Diamond Light Source. The selenium substructure was solved using SHELX and it is believed that this represents the first reported ab initio crystal structure to be solved using diffraction data collected at DLS.

Journal Keywords: Rsbs; Moorella Thermoacetica; Selenomethionine; Crystal Structure; Crystallization; Crystals; Diamonds; Diffraction; Diffusion; Light Sources; Mathematical Solutions; Proteins; Resolution; Selenium; Solutions; Space Groups

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

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