Open AccessCrystallization and preliminary X‐ray crystallographic studies of β‐transaminase from Mesorhizobium sp. strain LUK
Author(s) -
Kim Bokyung,
Park Ok Kyeung,
Bae Ju Young,
Jang Taeho,
Yoon Jong Hwan,
Do Kyoung Hun,
Kim ByungGee,
Yun Hyungdon,
Park Hyun Ho
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110050876
Subject(s) - strain (injury) , mesorhizobium , crystallization , crystallography , materials science , x ray , chemistry , biology , physics , nitrogen fixation , rhizobia , optics , organic chemistry , nitrogen , anatomy
β‐Transaminase (β‐TA) catalyzes the transamination reaction between β‐aminocarboxylic acids and keto acids. This enzyme is a particularly suitable candidate for use as a biocatalyst for the asymmetric synthesis of enantiochemically pure β‐amino acids for pharmaceutical purposes. The β‐TA from Mesorhizobium sp. strain LUK (β‐TA Ms ) belongs to a novel class in that it shows β‐transaminase activity with a broad and unique substrate specificity. In this study, β‐TA Ms was overexpressed in Escherichia coli with an engineered C‐terminal His tag. β‐TA Ms was then purified to homogeneity and crystallized at 293 K. X‐ray diffraction data were collected to a resolution of 2.5 Å from a crystal that belonged to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 90.91, b = 192.17, c = 52.75 Å.