Open AccessCrystallization and preliminary X‐ray analysis of a C‐terminal fragment of FlgJ, a putative flagellar rod cap protein from Salmonella
Author(s) -
Kikuchi Yuki,
Matsunami Hideyuki,
Yamane Midori,
Imada Katsumi,
Namba Keiichi
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108038207
Subject(s) - fragment (logic) , crystallization , crystallography , terminal (telecommunication) , protein crystallization , x ray , materials science , chemistry , physics , optics , computer science , organic chemistry , telecommunications , programming language
The formation of the bacterial flagellar axial structure, including the filament, the hook and the rod, requires the attachment of a cap complex to the distal end of the growing structure. Because the rod penetrates the peptidoglycan (PG) layer, the rod cap complex is thought to have PG‐hydrolyzing activity. FlgJ is a putative rod cap protein whose C‐terminal region shows sequence similarity to known muramidases. In this study, FlgJ 120–316 , a C‐terminal fragment of FlgJ which contains the muramidase region, was overproduced, purified and crystallized. Crystals were obtained by the sitting‐drop vapour‐diffusion technique using PEG 3350 as a crystallizing agent and belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 38.8, b = 43.9, c = 108.5 Å. Anomalous difference Patterson maps calculated from the diffraction data set of a selenomethionine‐labelled crystal showed significant peaks in the Harker sections, indicating that the data were suitable for structure determination.