These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Crystallization and preliminary X-ray diffraction analysis of a thermostable D-hydantoinase from the mesophilic Bacillus sp. AR9.
    Author: Agrawal V, Sharma R, Vohra RM, Kishan KV.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Dec; 58(Pt 12):2175-6. PubMed ID: 12454492.
    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.
    [Abstract] [Full Text] [Related] [New Search]