title: Purification, crystallization and preliminary X-ray diffraction analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus mutans strain UA159.
abstract: A triclosan-resistant flavoprotein termed FabK is the sole enoyl-acyl carrier protein reductase in Streptococcus pneumoniae and Streptococcus mutans. In this study, FabK from S. mutans strain UA159 was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.40 Å resolution using a synchrotron-radiation source. The crystal belonged to space group P6(2), with unit-cell parameters a = b = 105.79, c = 44.15 Å. The asymmetric unit contained one molecule, with a corresponding V(M) of 2.05 Å(3) Da(-1) and a solvent content of 39.9%.
authors.affiliation: Department of Chemistry, Konkuk University, 1 Hwayang-Dong, Gwangjin-Gu, Seoul 143-701, Republic of Korea.
authors.forename: Tae-O
authors.initials: TO
authors.lastname: Kim
authors.forename: Dong-Won
authors.initials: DW
authors.lastname: Im
authors.forename: Ha Yun
authors.initials: HY
authors.lastname: Jung
authors.forename: Seong Jung
authors.initials: SJ
authors.lastname: Kwon
authors.forename: Yong-Seok
authors.initials: YS
authors.lastname: Heo
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000302:isolation & purification; D013295:Streptococcus mutans / Q000201:enzymology*
chemical_list: D044925:Oxidoreductases Acting on CH-CH Group Donors