Crystallization and preliminary crystallographic studies of an active-site mutant hydantoin racemase from Sinorhizobium meliloti CECT4114
- Department of Cellular and Molecular Interactions, Vrije Universiteit Brussel, 1050 Brussels (Belgium)
- Laboratorio de Estudios Cristalográficos, IACT (CSIC-U. Granada), P. T. Ciencias de la Salud, Granada 18100 (Spain)
- Departamento de Química Física, Bioquímica y Química Inorgánica, Área de Bioquímica y Biología Molecular, Edf. CITE I, Universidad de Almería (Spain)
Crystals of an active-site mutated hydantoin racemase from S. meliloti have been obtained in the presence and absence of d,l-5-isopropyl-hydantoin and characterized by X-ray diffraction. A recombinant active-site mutant of hydantoin racemase (C76A) from Sinorhizobium meliloti CECT 4114 (SmeHyuA) has been crystallized in the presence and absence of the substrate d,l-5-isopropyl hydantoin. Crystals of the SmeHyuA mutant suitable for data collection and structure determination were grown using the counter-diffusion method. X-ray data were collected to resolutions of 2.17 and 1.85 Å for the free and bound enzymes, respectively. Both crystals belong to space group R3 and contain two molecules of SmeHyuA per asymmetric unit. The crystals of the free and complexed SmeHyuA have unit-cell parameters a = b = 85.43, c = 152.37 Å and a = b = 85.69, c = 154.38 Å, crystal volumes per protein weight (V{sub M}) of 1.94 and 1.98 Å{sup 3} Da{sup −1} and solvent contents of 36.7 and 37.9%, respectively.
- OSTI ID:
- 22360470
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 1; Other Information: PMCID: PMC2374001; PMID: 18097103; PUBLISHER-ID: nj5007; OAI: oai:pubmedcentral.nih.gov:2374001; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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