Crystallization and preliminary X-ray crystallographic analysis of ctxm-15,an extended-spectrum β-lactamase conferring worldwide emerging antibiotic resistance

Ctx-m-15,an extended-spectrum β-lactamase emerging worldwide,hydrolyzes lactam ring of β-lactam antibiotics,and thus causes therapeutic failure and a lack of eradication of pathogenic bacteria by third-generation β-lactams. therefore,the enzyme is a potential target for developing agents against pathogens isolated from patients suffering from nosocomial infections. the ctx-m-15 protein was purified and crystallized at 298 k. x-ray diffraction data from ctxm-15 crystal have been collected to 1.46 å resolution using synchrotron radiation. the crystal of ctx-m-15 belongs to space group p2 12 12 1,with unit-cell parameters a = 45.50,b = 44.23,and c = 116.92 å. analysis of the packing density shows that the asymmetric unit probably contains two molecules with a solvent content of 41.26%. © 2011 bentham science publishers ltd.