Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of the C‐terminal cytoplasmic domain of FlhB from Salmonella typhimurium
Author(s) -
Meshcheryakov Vladimir A.,
Samatey Fadel A.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111018938
Subject(s) - cytoplasm , crystallization , crystallography , domain (mathematical analysis) , resolution (logic) , salmonella , transmembrane domain , transmembrane protein , chemistry , physics , biology , membrane , bacteria , biochemistry , genetics , mathematics , mathematical analysis , organic chemistry , computer science , receptor , 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). FlhBc from Salmonella typhimurium has been successfully crystallized using the vapour‐diffusion method. The crystals diffracted to 2.45 Å resolution and belonged to space group P 4 2 2 1 2, with unit‐cell parameters a = b = 49.06, c = 142.94 Å. A selenomethionine‐containing variant of FlhBc has also been crystallized in the same space group and was used for initial phase calculation by the multiwavelength anomalous dispersion (MAD) method.