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• W3024173746 startingPage "165" @default.
• W3024173746 abstract "Bacteriophages produce endolysins that target and cleave the hosts peptidoglycan to release their progeny at the end of the infection cycle. These proteins can be used for the eradication of pathogenic bacteria, but also for their detection. Endolysins may contain a single catalytic domain or several domains, including a cell wall binding domain. To understand their function in detail and design mutated or chimeric molecules with novel properties, knowledge of their structures and detailed mechanisms is necessary. X-ray protein crystallography is an excellent method to obtain high-resolution structures of biological macromolecules, and here we describe the method and the folds of known endolysin domains." @default.
• W3024173746 created "2020-05-21" @default.
• W3024173746 creator A5026557929 @default.
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• W3024173746 date "2021-01-01" @default.
• W3024173746 modified "2023-09-25" @default.
• W3024173746 title "Crystallographic Structure Determination of Bacteriophage Endolysins" @default.
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• W3024173746 doi "https://doi.org/10.21775/cimb.040.165" @default.
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• W3024173746 hasPublicationYear "2021" @default.
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