Crystal structure of elastase–substrate complex at −55 °C
- 1 September 1976
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 263 (5575), 297-300
- https://doi.org/10.1038/263297a0
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 Å resolution. The acyl-enzyme was stabilised by cooling the crystal to −55°C during substrate addition and data collection.This publication has 24 references indexed in Scilit:
- Formation of stable crystalline enzyme–substrate intermediates at sub-zero temperaturesNature, 1976
- Cryoenzymology of chymotrypsin: the detection of intermediates in the catalysis of a specific anilide substrateBiochemistry, 1976
- Protein crystallography at sub-zero temperatures: Lysozyme-substrate complexes in cooled mixed solventsJournal of Molecular Biology, 1975
- High resolution nuclear magnetic resonance studies of the active site of chymotrypsin: II. Polarization of histidine 57 by substrate analogues and competitive inhibitorsJournal of Molecular Biology, 1974
- Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteasesBiochemistry, 1973
- Enzymology at sub-zero temperaturesMolecular and Cellular Biochemistry, 1973
- Aqueous-organic solutions of enzymes at sub-zero temperaturesBiochimie, 1971
- Le contrôle thermique des réactions enzymatiquesBiochimie, 1971
- Temporal Resolution of Individual Steps in an Enzymic Reaction at Low TemperatureProceedings of the National Academy of Sciences, 1970
- X-Ray Diffraction Studies of EnzymesAnnual Review of Biochemistry, 1970