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

Wen-Hwei Hsu, Fan-Tso Chien, Chuan-Long Hsu, Tse-Chi Wang,  Hanna S. Yuan and Wen-Ching Wang

SUMMARY 

The Agrobacterium radiobacter CCRC 14924 N-carbamyl-d-amino-acid amidohydrolase, the enzyme used for production of d-amino acids, was overexpressed in Escherichia coli JM109. The expressed protein was crystallized by vapour diffusion using lithium sulfate as precipitant. It crystallizes in space group P21 with unit-cell parameters a = 69.8, b = 67.9 and c = 137.8  Å and ß = 96.4. There are four molecules per asymmetric unit. Crystals diffract to 2.8 Å resolution using a rotating-anode source at cryogenic (113 K) temperatures.

Acta Cryst. (1999). D55, 694-695