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Active Site Geometries for a Family of Metallo-beta-Lactamases

dc.contributor.authorPage, Richard
dc.contributor.authorWolke, Will
dc.date.accessioned2025-09-16T14:33:38Z
dc.date.available2025-09-16T14:33:38Z
dc.identifier.urihttp://hdl.handle.net/2374.MIA/7052
dc.description.abstractInitial results from an analysis for a set of 84 metallo-beta-lactamase enzymes examining the internuclear distance between each zinc and each interacting atom, and the possible sets of angles formed by three atoms in which the central atom of the trio is one of the active site zinc ions.en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.titleActive Site Geometries for a Family of Metallo-beta-Lactamasesen_US
dc.typeOtheren_US


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  • Page, Richard
    Dr. Richard Page - Associate Professor, Department of Chemistry and Biochemistry

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