Open AccessCrystallization and preliminary crystallographic studies of an active‐site mutant hydantoin racemase from Sinorhizobium meliloti CECT4114
Author(s) -
MartínezRodríguez Sergio,
GonzálezRamírez Luis Antonio,
ClementeJiménez Josefa María,
RodríguezVico Felipe,
Las HerasVázquez Francisco Javier,
Gavira Jose Antonio,
GarcíaRuiz Juan Ma.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107066122
Subject(s) - hydantoin , crystallization , sinorhizobium meliloti , crystallography , mutant , stereochemistry , crystal structure , chemistry , biochemistry , organic chemistry , gene
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 R 3 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 M ) of 1.94 and 1.98 Å 3 Da −1 and solvent contents of 36.7 and 37.9%, respectively.