title: Crystallization and preliminary X-ray analysis of betaC-S lyases from two oral Streptococci.
abstract: Hydrogen sulfide, which causes oral malodour, is generally produced from L-cysteine by the action of betaC-S lyase from oral bacteria. The betaC-S lyases from two oral bacteria, Streptococcus anginosus and S. gordonii, have been cloned, overproduced, purified and crystallized. X-ray diffraction data were collected from the two types of crystals using synchrotron radiation. The crystal of S. anginosus betaC-S lyase belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 111.1, c = 216.4 A, and the crystal of S. gordonii betaC-S lyase belonged to the same space group, with unit-cell parameters a = 58.0, b = 73.9. c = 187.6 A. The structures of the betaC-S lyases were solved by molecular-replacement techniques.
authors.affiliation: Department of Structural Biology, School of Pharmacy, Iwate Medical University, Yahaba, Iwate 028-3694, Japan.
authors.forename: Yuichiro
authors.initials: Y
authors.lastname: Kezuka
authors.forename: Yasuo
authors.initials: Y
authors.lastname: Yoshida
authors.forename: Takamasa
authors.initials: T
authors.lastname: Nonaka
mesh_terms: D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D008190:Lyases / Q000737:chemistry*; D009055:Mouth / Q000382:microbiology*; D012399:Rotation; D034366:Streptococcus anginosus / Q000201:enzymology*; D054773:Streptococcus gordonii / Q000201:enzymology*
chemical_list: D008190:Lyases; C019965:cystathionine beta-lyase