Open AccessCrystallization and preliminary X‐ray analysis of βC–S lyases from two oral streptococci
Author(s) -
Kezuka Yuichiro,
Yoshida Yasuo,
aka Takamasa
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109030371
Subject(s) - orthorhombic crystal system , lyase , streptococcus gordonii , crystallography , crystallization , bacteria , chemistry , crystal (programming language) , crystal structure , streptococcus , biology , biochemistry , enzyme , genetics , organic chemistry , computer science , programming language
Hydrogen sulfide, which causes oral malodour, is generally produced from l ‐cysteine by the action of βC–S lyase from oral bacteria. The βC–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 βC–S lyase belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 67.0, b = 111.1, c = 216.4 Å, and the crystal of S. gordonii βC–S lyase belonged to the same space group, with unit‐cell parameters a = 58.0, b = 73.9. c = 187.6 Å. The structures of the βC–S lyases were solved by molecular‐replacement techniques.