Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C beta-lactamases with extended substrate spectrum

Abstract

Plasmid-encoded class C beta-lactamases, including CMY-1 and CMY-10, hydrolyze the lactam bonds of beta-lactam antibiotics, inducing therapeutic failure and a lack of eradication of clinical isolates by third-generation cephalosporins or cephamycins. Therefore, the enzymes are potential targets for developing agents against pathogens isolated from patients suffering from wound infection, urinary tract infection or pneumonia. CMY-1 and CMY-10 were purified and crystallized at 298 K. X-ray diffraction data from CMY-1 and CMY-10 crystals have been collected to 2.5 and 1.5 Angstrom resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P2(1).