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Crystallization and preliminary crystallographic studies of an active-site mutant hydantoin racemase from Sinorhizobium meliloti CECT4114.

AuthorsMartínez-Rodríguez, S.; González-Ramírez, L. A.; Clemente-Jiménez, J. M.; Rodríguez-Vico, F.; Las Heras-Vázquez, F. J.; Gavira Gallardo, J. A. ; García Ruiz, Juan Manuel
KeywordsHydantoin racemase
Sinorhizobium meliloti
D,L-5-isopropyl hydantoin
Issue DateJan-2008
PublisherInternational Union of Crystallography
CitationActa Cryst. 64(1): 50-53 (2008)
AbstractA 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.
Publisher version (URL)http://dx.doi.org/10.1107/S1744309107066122
Appears in Collections:(IACT) Artículos
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