title: Crystallization and preliminary X-ray diffraction studies of a novel alkaline serine protease (KP-43) from alkaliphilic Bacillus sp. strain KSM-KP43.
abstract: A novel alkaline serine protease (KP-43) which belongs to a new class of the subtilisin superfamily was crystallized by the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 43.50 (2), b = 110.4 (1), c = 168.9 (1) A. The crystals diffract X-rays beyond 1.9 A resolution using Cu Kalpha radiation from a rotating-anode generator and are suitable for high-resolution crystal structure analysis.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nonaka
authors.forename: M
authors.initials: M
authors.lastname: Fujihashi
authors.forename: A
authors.initials: A
authors.lastname: Kita
authors.forename: K
authors.initials: K
authors.lastname: Saeki
authors.forename: S
authors.initials: S
authors.lastname: Ito
authors.forename: K
authors.initials: K
authors.lastname: Miki
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006863:Hydrogen-Ion Concentration; D012697:Serine Endopeptidases / Q000737:chemistry*
chemical_list: D012697:Serine Endopeptidases