title: Crystallization and preliminary X-ray analysis of the catalytic domain of chitinase D from Bacillus circulans WL-12.
abstract: We report here on crystallization and preliminary X-ray analysis of the catalytic domain of chitinase D from Bacillus circulans WL-12. The native crystals of this domain were found to belong to the orthorhombic space group P2(1)2(1)2(1). To elucidate the structure of the catalytic domain by the multiple isomorphous replacement method, 30 kinds of derivatized crystals were prepared by soaking the native crystals into a mother liquor containing salts of heavy metal atoms. Difference Patterson maps calculated for four derivatives showed strong peaks in the Harker sections.
authors.affiliation: Department of BioEngineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
authors.forename: Yuichiro
authors.initials: Y
authors.lastname: Kezuka
authors.forename: Kenji
authors.initials: K
authors.lastname: Bando
authors.forename: Hajime
authors.initials: H
authors.lastname: Kobayashi
authors.forename: Yasuo
authors.initials: Y
authors.lastname: Yonou
authors.forename: Toshiya
authors.initials: T
authors.lastname: Sato
authors.forename: Takeshi
authors.initials: T
authors.lastname: Watanabe
authors.forename: Takamasa
authors.initials: T
authors.lastname: Nonaka
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D002688:Chitinases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D007527:Isoenzymes / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D007527:Isoenzymes; D002688:Chitinases