Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter

Citation
Wh. Hsu et al., Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter, ACT CRYST D, 55, 1999, pp. 694-695
Citations number
12
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
3
Pages
694 - 695
Database
ISI
SICI code
0907-4449(199903)55:<694:ECAPXD>2.0.ZU;2-K
Abstract
The Agrobacterium radiobacter CCRC 14924 N-carbamyl-D-amino-acid amidohydro lase, the enzyme used for production of D-amino acids, was overexpressed in Escherichia coli JM109. The expressed protein was crystallized by vapour d iffusion using lithium sulfate as precipitant. It crystallizes in space gro up P2(1) with unit-cell parameters cr = 69.8, b = 67.9 and c = 137.8 Angstr om and beta = 96.4 degrees. There are four molecules per asymmetric unit. C rystals diffract to 2.8 Angstrom resolution using a rotating-anode source a t cryogenic (113 K) temperatures.