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DC Field | Value | Language |
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dc.citation.endPage | 384 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 382 | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | - |
dc.citation.volume | 60 | - |
dc.contributor.author | Lee, SJ | - |
dc.contributor.author | Kim, JY | - |
dc.contributor.author | Jung, HI | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Lee, HS | - |
dc.contributor.author | Lee, SH | - |
dc.contributor.author | Cha, SS | - |
dc.date.accessioned | 2023-12-22T11:07:05Z | - |
dc.date.available | 2023-12-22T11:07:05Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2004-02 | - |
dc.description.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 A resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P21. | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.60, no.2, pp.382 - 384 | - |
dc.identifier.doi | 10.1107/S090744490302821X | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.scopusid | 2-s2.0-4644281606 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5612 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=4644281606 | - |
dc.identifier.wosid | 000188428900038 | - |
dc.language | 영어 | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.title | Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C beta-lactamases with extended substrate spectrum | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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