2024-03-28T18:39:22Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/184002022-11-29T08:54:43Zcom_10261_91com_10261_8col_10261_344
DIGITAL.CSIC
author
Martínez-Rodríguez, Sergio
author
González-Ramírez, L. A.
author
Clemente-Jiménez, J. M.
author
Rodríguez-Vico, F.
author
Las Heras-Vázquez, F. J.
author
Gavira Gallardo, J. A.
author
García Ruiz, Juan Manuel
2009-11-10T09:13:08Z
2009-11-10T09:13:08Z
2008-01
Acta Cryst. 64(1): 50-53 (2008)
1744-3091
http://hdl.handle.net/10261/18400
10.1107/S1744309107066122
18097103
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 (VM) of 1.94 and 1.98 Å3 Da-1 and solvent contents of 36.7 and 37.9%, respectively.
eng
closedAccess
Hydantoin racemase
Sinorhizobium meliloti
D,L-5-isopropyl hydantoin
Crystallization and preliminary crystallographic studies of an active-site mutant hydantoin racemase from Sinorhizobium meliloti CECT4114.
artículo
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