Crystallization and preliminary X-ray crystallographic studies of omega-transaminase from Vibrio fluvialis JS17

Omega-transaminase (ω-TA) catalyzes the transfer of an amino group from a non-α-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, ω-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 Å from a crystal belonging to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 78.43, b = 95.95, c = 122.89 Å.