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

Sun Joo Lee, Young Kim Jae, Il Jung Ha, Pann Ghill Suh, Heung Soo Lee, Hee Lee Sang, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Plasmid-encoded class C β-lactamases, including CMY-1 and CMY-10, hydrolyze the lactam bonds of β-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 Å resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P21.

Original languageEnglish
Pages (from-to)382-384
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number2
DOIs
StatePublished - Feb 2004

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