Purification, crystallization and preliminary X-ray analysis of the beta-lactamase Oih-1 from Oceanobacillus iheyensis.
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).
Toth
Marta
M
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Vakulenko
Sergei B
SB
Smith
Clyde A
CA
D000595:Amino Acid Sequence; D001406:Bacillaceae / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D003625:Data Collection; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D012399:Rotation; D017386:Sequence Homology, Amino Acid; D013223:Statistics as Topic; D017356:Synchrotrons; D014961:X-Ray Diffraction; D001618:beta-Lactamases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
D001426:Bacterial Proteins; D001618:beta-Lactamases