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
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.