Open AccessCrystallization and preliminary X‐ray analysis of FlgA, a periplasmic protein essential for flagellar P‐ring assembly
Author(s) -
Matsunami Hideyuki,
Samatey Fadel A.,
Nagashima Shigehiro,
Imada Katsumi,
Namba Keiichi
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112001327
Subject(s) - periplasmic space , crystallization , crystallography , resolution (logic) , crystal (programming language) , ring (chemistry) , protein crystallization , molecule , solvent , diffraction , materials science , crystal structure , chemistry , physics , optics , escherichia coli , organic chemistry , biochemistry , artificial intelligence , computer science , gene , programming language
Salmonella FlgA, a periplasmic protein essential for flagellar P‐ring assembly, has been crystallized in two forms. The native protein crystallized in space group C 222, with unit‐cell parameters a = 107.5, b = 131.8, c = 49.4 Å, and diffracted to about 2.0 Å resolution (crystal form I). In this crystal, the asymmetric unit is likely to contain one molecule, with a solvent content of 66.8%. Selenomethionine‐labelled FlgA protein crystallized in space group C 222 1 , with unit‐cell parameters a = 53.2, b = 162.5, c = 103.5 Å, and diffracted to 2.7 Å resolution (crystal form II). In crystal form II, the asymmetric unit contained two molecules with a solvent content of 48.0%. The multiple‐wavelength and single‐wavelength anomalous dispersion methods allowed the visualization of the electron‐density distributions of the form I and II crystals, respectively. The two maps suggested that FlgA is in two different conformations in the two crystals.