title: Crystallization and preliminary X-ray analysis of FlgA, a periplasmic protein essential for flagellar P-ring assembly.
abstract: Salmonella FlgA, a periplasmic protein essential for flagellar P-ring assembly, has been crystallized in two forms. The native protein crystallized in space group C222, 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 C222(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.
authors.affiliation: Dynamic NanoMachine Project, ICORP, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Matsunami
authors.forename: Fadel A
authors.initials: FA
authors.lastname: Samatey
authors.forename: Shigehiro
authors.initials: S
authors.lastname: Nagashima
authors.forename: Katsumi
authors.initials: K
authors.lastname: Imada
authors.forename: Keiichi
authors.initials: K
authors.lastname: Namba
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D012475:Salmonella / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; C087497:FlgA protein, Salmonella