title: Crystallization and preliminary X-ray crystallographic studies of ω-transaminase from Vibrio fluvialis JS17.
abstract: Omega-transaminase (ω-TA) catalyzes the transfer of an amino group from a non-alpha-position amino acid or an amine compound with no carboxylic group to an amino acceptor. ω-TA from Vibrio fluvialis JS17 (ω-TAVf) is a novel amine:pyruvate transaminase that is capable of stereoselective transamination of aryl chiral amines. In this study, omega-TAVf was overexpressed in Escherichia coli with engineered C-terminal His tags. ω-TAVf was then purified to homogeneity and crystallized at 292 K. X-ray diffraction data were collected to a resolution of 2.5 A from a crystal belonging to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=78.43, b=95.95, c=122.89 A.
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry at Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Tae-ho
authors.initials: TH
authors.lastname: Jang
authors.forename: Bokyung
authors.initials: B
authors.lastname: Kim
authors.forename: Ok Kyoung
authors.initials: OK
authors.lastname: Park
authors.forename: Ju Young
authors.initials: JY
authors.lastname: Bae
authors.forename: Byung-Gee
authors.initials: BG
authors.lastname: Kim
authors.forename: Hyungdon
authors.initials: H
authors.lastname: Yun
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D000637:Transaminases / Q000737:chemistry*; D014733:Vibrio / Q000201:enzymology*
chemical_list: D000637:Transaminases