title: Purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytoplasmic domain of FlhB from Aquifex aeolicus.
abstract: 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 C2, with unit-cell parameters a = 114.49, b = 33.89, c = 122.13 Å, β = 107.53°.
authors.affiliation: Trans-Membrane Trafficking Unit, Okinawa Institute of Science and Technology, Kunigami-gun, Okinawa, Japan.
authors.forename: Vladimir A
authors.initials: VA
authors.lastname: Meshcheryakov
authors.forename: Young-Ho
authors.initials: YH
authors.lastname: Yoon
authors.forename: Fadel A
authors.initials: FA
authors.lastname: Samatey
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D003593:Cytoplasm; D004058:Diffusion; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; C085668:FlhB protein, Bacteria; D008565:Membrane Proteins