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S.P. Tolley

Researcher at University of York

Publications -  15
Citations -  2203

S.P. Tolley is an academic researcher from University of York. The author has contributed to research in topics: Crystallization & Multiple isomorphous replacement. The author has an hindex of 10, co-authored 15 publications receiving 2152 citations. Previous affiliations of S.P. Tolley include New York University.

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A serine protease triad forms the catalytic centre of a triacylglycerol lipase.

TL;DR: The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
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Penicillin acylase has a single-amino-acid catalytic centre.

TL;DR: The analysis shows that the environment of the catalytically active N-terminal serine of the B chain contains no adjacent histidine equivalent to that found in the serine proteases, indicating that this must be an important recognition site for cleavage.
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The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase

TL;DR: Crystallographic data is presented on a possible product complex between CBG and glucose, resulting from co-crystallization of the native enzyme with its natural substrate, linamarin, using multiple isomorphous replacement.
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Structures of oligosaccharide-bound forms of the endoglucanase v from humicola insolens at 1.9 a resolution

TL;DR: Endoglucanase V, from the cellulolytic soil hyphomycete Humicola insolens, is an endocellulase, the catalytic core of which consists of 210 amino acids and is known to hydrolyze the beta-1,4 links with inversion of configuration at the anomeric carbon.
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Structure and function of endoglucanase V

TL;DR: A third cellulase, endoglucanase V, is reported, structurally distinct from the previously determined cellulases but is similar to a recently characterized plant defence protein, despite the lack of structural similarity between these two enzymes.