Work

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

Year: 2009

Type: article

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).

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309109015759

Authors: Marta Toth, Sergei B. Vakulenko, Clyde A. Smith

Institutions: University of Notre Dame, Stanford Synchrotron Radiation Lightsource, Stanford University

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funders: National Institute of Allergy and Infectious Diseases, National Center for Research Resources

Awards: G113944070, G1321237418, G4721672654, G5455679053