TY  - JOUR
N1  - Copyright of this article belongs to Wiley.


ID  - open256
UR  - http://journals.iucr.org/d/issues/2002/12/00/pu0067/pu0067.pdf
IS  - Pt 12
A1  - Agrawal, Vishal
A1  - Sharma, Rakesh
A1  - Vohra, R M
A1  - Kishan, K V Radha
Y1  - 2002/12//
N2  - 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.
PB  - International Union of Microbiological Societies/ Wiley
JF  - Acta crystallographica. Section D, Biological crystallography
VL  - 58
SN  - 0907-4449
TI  - Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.
SP  - 2175
AV  - restricted
EP  - 6
ER  -