creators_name: Agrawal, Vishal
creators_name: Sharma, Rakesh
creators_name: Vohra, R M
creators_name: Kishan, K V Radha
type: article
datestamp: 2012-01-05 15:06:53
lastmod: 2015-01-09 10:54:25
metadata_visibility: show
title: Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.
ispublished: pub
subjects: QD
full_text_status: restricted
note: Copyright of this article belongs to Wiley.


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.
date: 2002-12
date_type: published
publication: Acta crystallographica. Section D, Biological crystallography
volume: 58
number: Pt 12
publisher: International Union of Microbiological Societies/ Wiley
pagerange: 2175-6
refereed: TRUE
issn: 0907-4449
official_url: http://journals.iucr.org/d/issues/2002/12/00/pu0067/pu0067.pdf
related_url_url: http://journals.iucr.org/d/issues/2002/12/00/pu0067/pu0067.pdf
related_url_type: pub
citation:   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     
document_url: http://crdd.osdd.net/open/256/1/kishan2002.2.pdf