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PMID: 958484 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Crystal structure of elastase-substrate complex at -- 55 degrees C.

Nature ·Vol. 263 ·No. 5575 ·1976-09-23 ·Pages 297-300

Alber T, Petsko GA, Tsernoglou D

Abstract

The structure of a specific acyl-enzyme intermediate in the elastase-catalysed hydrolysis of N-carbobenzoxy-L-alanyl-p-nitrophenol ester has been determined by X-ray diffraction at 3.5 A resolution. The acyl-enzyme was stabilised by cooling the crystal to --55 degrees C during substrate addition and data collection.

MeSH Terms

Binding Sites Cold Temperature Crystallization Nitrophenols/metabolism Pancreatic Elastase/metabolism Protein Conformation X-Ray Diffraction

Chemicals

Nitrophenols Pancreatic Elastase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Alber T

Petsko G A

Tsernoglou D

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/263297a0

Published

1976-09-23

Pages

297-300

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/263297a0 View journal details

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Crystal structure of elastase-substrate complex at -- 55 degrees C.

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