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

ABSTRACT: Bacterial resistance to the beta-lactam family of antibiotics is primarily the result of the deactivation of the drugs by beta-lactamase enzymes. The gene encoding the proficient beta-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 P3(1)21 but with distinctly different unit-cell parameters. Synchrotron diffraction data were collected to high resolution (1.65-1.75 A) from both crystal forms on beamlines BL7-1 and BL11-1 at SSRL (Stanford, California, USA).

SUBMITTER: Toth M

PROVIDER: S-EPMC2688415 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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

Toth Marta M Vakulenko Sergei B SB Smith Clyde A CA

Acta crystallographica. Section F, Structural biology and crystallization communications 20090522 Pt 6

Bacterial resistance to the beta-lactam family of antibiotics is primarily the result of the deactivation of the drugs by beta-lactamase enzymes. The gene encoding the proficient beta-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 ...[more]

PMID: 19478436

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