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Purification, crystallization and preliminary X‐ray crystallographic analysis of the C‐terminal cytoplasmic domain of FlhB from Aquifex aeolicus

Purification, crystallization and preliminary X‐ray crystallographic analysis of the C‐terminal... FlhB is a key protein in the regulation of protein export by the bacterial flagellar secretion system. It is composed of two domains: an N‐terminal transmembrane domain and a C‐terminal cytoplasmic domain (FlhBc). Here, the crystallization and preliminary crystallographic analysis of FlhBc from Aquifex aeolicus are reported. Purified protein was crystallized using the vapour‐diffusion technique. The crystals diffracted to 2.3 Å resolution and belonged to space group C2, with unit‐cell parameters a = 114.49, b = 33.89, c = 122.13 Å, β = 107.53°. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Purification, crystallization and preliminary X‐ray crystallographic analysis of the C‐terminal cytoplasmic domain of FlhB from Aquifex aeolicus

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References (17)

Publisher
Wiley
Copyright
International Union of Crystallography, 2011
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309110052942
pmid
21301106
Publisher site
See Article on Publisher Site

Abstract

FlhB is a key protein in the regulation of protein export by the bacterial flagellar secretion system. It is composed of two domains: an N‐terminal transmembrane domain and a C‐terminal cytoplasmic domain (FlhBc). Here, the crystallization and preliminary crystallographic analysis of FlhBc from Aquifex aeolicus are reported. Purified protein was crystallized using the vapour‐diffusion technique. The crystals diffracted to 2.3 Å resolution and belonged to space group C2, with unit‐cell parameters a = 114.49, b = 33.89, c = 122.13 Å, β = 107.53°.

Journal

Acta Crystallographica Section FWiley

Published: Feb 1, 2011

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