Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of the C‐terminal cytoplasmic domain of FlhB from Aquifex aeolicus
Author(s) -
Meshcheryakov Vladimir A.,
Yoon YoungHo,
Samatey Fadel A.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110052942
Subject(s) - aquifex aeolicus , crystallization , crystallography , domain (mathematical analysis) , transmembrane domain , cytoplasm , resolution (logic) , diffraction , transmembrane protein , chemistry , materials science , physics , escherichia coli , amino acid , optics , biochemistry , gene , computer science , mathematics , mathematical analysis , receptor , organic chemistry , artificial intelligence
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 C 2, with unit‐cell parameters a = 114.49, b = 33.89, c = 122.13 Å, β = 107.53°.