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Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.
 
Creator Agrawal, Vishal
Sharma, Rakesh
Vohra, R M
Kishan, K V Radha
 
Subject QD Chemistry
 
Description 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.
 
Publisher International Union of Microbiological Societies/ Wiley
 
Date 2002-12
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/256/1/kishan2002.2.pdf
Agrawal, Vishal and Sharma, Rakesh and Vohra, R M and Kishan, K V Radha (2002) Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9. Acta crystallographica. Section D, Biological crystallography, 58 (Pt 12). pp. 2175-6. ISSN 0907-4449
 
Relation http://journals.iucr.org/d/issues/2002/12/00/pu0067/pu0067.pdf
http://crdd.osdd.net/open/256/