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Crystallization and Preliminary X-Ray Crystallographic Analysis of CTXM- 15, an Extended-spectrum β-Lactamase Conferring Worldwide Emerging Antibiotic Resistance

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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 P212121, 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%.

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Keywords: Antibiotic resistance; Asp240Gly mutation; CTX-M-15; Cephalosporins; ESBLs; Escherichia coli; Polyethylene glycol; Polymerase chain reaction; antibiotics; cefotaxime; ceftazidime; crystal; extended-spectrum β-lactamase; lactam ring; liquid nitrogen; nosocomial infections; oxyimino β-lactams; polyacrylamide SDS gel; synchrotron radiation; third-generation β-lactams; variants

Document Type: Research Article

Publication date: September 1, 2011

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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