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dc.contributor.authorMarshall, A.-
dc.contributor.authorKeiller, B.-
dc.contributor.authorPederick, J.-
dc.contributor.authorAbell, A.-
dc.contributor.authorBruning, J.-
dc.contributor.editorWu, A.-
dc.identifier.citationCrystals, 2018; 8(12):460-460-
dc.description.abstractChymotrypsin is a protease that is commonly used as a standard for protein crystallization and as a model system for studying serine proteases. Unliganded bovine α-chymotrypsin was crystallized at neutral pH using ammonium sulphate as the precipitant, resulting in crystals that conform to P65 symmetry with unit cell parameters that have not been reported previously. Inspection of crystallographic interfaces revealed that the major interface between any two molecules in the crystal lattice represents the interface of the biological dimer, as previously observed for crystals of unliganded α-chymotrypsin grown at low pH in space group P21.-
dc.description.statementofresponsibilityAndrew C. Marshall, Benjamin G. Keiller, Jordan L. Pederick, Andrew D. Abell and John B. Bruning-
dc.rights© 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (
dc.subjectTrypsin-like serine protease; endopeptidase; hydrolase-
dc.titleCrystal structure of bovine alpha-chymotrypsin in space group P65-
dc.typeJournal article-
dc.identifier.orcidMarshall, A. [0000-0002-9770-4594]-
dc.identifier.orcidPederick, J. [0000-0003-4048-9771]-
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]-
dc.identifier.orcidBruning, J. [0000-0002-6919-1824]-
Appears in Collections:Aurora harvest 3
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