title: Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.
abstract: 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.
authors.affiliation: Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036, India.
authors.forename: Vishal
authors.initials: V
authors.lastname: Agrawal
authors.forename: Rakesh
authors.initials: R
authors.lastname: Sharma
authors.forename: Rakesh M
authors.initials: RM
authors.lastname: Vohra
authors.forename: K V Radha
authors.initials: KV
authors.lastname: Kishan
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry*; D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D011487:Protein Conformation; D013237:Stereoisomerism
chemical_list: D000581:Amidohydrolases; C020047:dihydropyrimidinase