Crystallization and preliminary crystallographic studies of an active-site mutant hydantoin racemase fromSinorhizobium melilotiCECT4114

descriptionPublicationkeyboard_double_arrow_right Article 20 Dec 2007 Spain Publisher:International Union of Crystallography (IUCr)Journal:Acta Crystallographica Section F Structural Biology and Crystallization Communications, volume 64, pages 50-53 (eissn: 1744-3091,

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Authors: Martínez Rodríguez, Sergio; Gonzalez Ramirez, L.A.; Clemente Jiménez, Josefa María; Rodríguez Vico, Felipe; Las Heras Vázquez, Francisco Javier; Gavira, J.A.; Garcia Ruiz, J.M.;

doi: 10.1107/s1744309107066122

pmid: 18097103

pmc: PMC2374001

handle: 10261/18400 , 10835/16553

Crystallization and preliminary crystallographic studies of an active-site mutant hydantoin racemase fromSinorhizobium melilotiCECT4114

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Abstract

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 A 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 A and a = b = 85.69, c = 154.38 A, crystal volumes per protein weight (V(M)) of 1.94 and 1.98 A3 Da(-1) and solvent contents of 36.7 and 37.9%, respectively.

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Spain

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Keywords

Binding Sites, Bacterial Proteins, Racemases and Epimerases, Indicators and Reagents, Hydantoin racemase, Crystallization, D,L-5-isopropyl hydantoin, Recombinant Proteins, Sinorhizobium meliloti

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