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Start Over Author "Chien FT" Journal acta crystallographica section d biological crystallography

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

Author

Hsu WH, Chien FT, Hsu CL, Wang TC, Yuan HS, and Wang WC

Subjects
Amidohydrolases genetics, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Escherichia coli genetics, Protein Conformation, Amidohydrolases chemistry, Rhizobium enzymology
Abstract

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 A and beta = 96.4 degrees. There are four molecules per asymmetric unit. Crystals diffract to 2.8 A resolution using a rotating-anode source at cryogenic (113 K) temperatures.

Published
1999
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