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Crystal quality and inhibitor binding by aspartic proteinases; preparation of high quality crystals of mouse renin

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Renin from mouse submandibular glands has been highly purified and co-crystallized with a synthetic nonapeptide fragment of rat angiotensionogen in which the scissile Leu-Leu bond has been modified as a hydroxyethylene mimic of the transition state. The strong diffraction from these crystals compared to the native form is discussed in relation to the behaviour of other members of the aspartic proteinase family in crystallisation.
Original languageEnglish
Pages (from-to)393-399
JournalJournal of Crystal Growth
Volume122
Issue number1-4
DOIs
Publication statusPublished - 1 Aug 1992

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