Purification, crystallization and preliminary X-ray analysis of the β-lactamase Oih-1 from Oceanobacillus iheyensis

Abstract

Bacterial resistance to the β-lactam family of antibiotics is primarily the result of the deactivation of the drugs by β-lactamase enzymes. The gene encoding the proficient β-lactamase Oih-1 from the alkaliphilic and halotolerant Gram-positive bacterium Oceanobacillus iheyensis has been cloned and the mature wild-type protein (comprising 274 amino-acid residues) has been expressed in Escherichia coli and subsequently purified to homogeneity. Oih-1 crystallized in two crystal forms both belonging to the trigonal space group P3121 but with distinctly different unit-cell parameters. Synchrotron diffraction data were collected to high resolution (1.65-1.75 Å) from both crystal forms on beamlines BL7-1 and BL11-1 at SSRL (Stanford, California, USA). © 2009 International Union of Crystallography. All rights reserved.