Open AccessPurification, crystallization and preliminary X‐ray analysis of the β‐lactamase Oih‐1 from Oceanobacillus iheyensis
Author(s) -
Toth Marta,
Vakulenko Sergei B.,
Smith Clyde A.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109015759
Subject(s) - escherichia coli , crystallization , crystallography , bacteria , halotolerance , crystal structure , chemistry , x ray , enzyme , microbiology and biotechnology , gene , biology , biochemistry , genetics , physics , optics , organic chemistry
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 P 3 1 21 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).