Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.
D-hydantoinase catalyzes the conversion of DL-hydantoin derivatives to the corresponding optically pure N-carbamoyl amino acids, the first step in the industrial preparation of optically pure amino acids using biological catalysts. A thermostable D-hydantoinase from the mesophilic bacteria Bacillus sp. AR9 has been crystallized in three different crystal forms. The hexagonal faced crystals were the best looking, but did not diffract. One of the crystal forms is star-shaped and appeared to be twinned, but diffracted as a single crystal to a resolution of 2.3 A. These crystals belong to space group P6(4) and have unit-cell parameters a = b = 129.55, c = 102.86 A, alpha = beta = 90, gamma = 120 degrees.
Agrawal
Vishal
V
Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036, India.
Sharma
Rakesh
R
Vohra
Rakesh M
RM
Kishan
K V Radha
KV
D000581:Amidohydrolases / Q000737:chemistry*; D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D011487:Protein Conformation; D013237:Stereoisomerism
D000581:Amidohydrolases; C020047:dihydropyrimidinase