Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
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Publisher
London: Nature Publishing Group UK
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Language
English
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Publisher
London: Nature Publishing Group UK
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Serial x-ray crystallography can uncover binding events, and subsequent chemical conversions occurring during enzymatic reaction. Here, we reveal the structure, binding and cleavage of moxalactam antibiotic bound to L1 metallo-β-lactamase (MBL) from
Stenotrophomonas maltophilia
. Using time-resolved serial synchrotron crystallography, we show...
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Full title
Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
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TN_cdi_doaj_primary_oai_doaj_org_article_80797d0f7a5c41ea943dfc5308b435e3
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_80797d0f7a5c41ea943dfc5308b435e3
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-022-35029-3
