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A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin

Record type: Article

Until now, no aspartic proteinase has been subjected to a successful neutron diffraction analysis, owing to the limited size of the crystals. However, the recent development of the neutron Laue technique at ILL and EMBL (Grenoble) has allowed the collection of data to 2.2 Å on a complex of endothiapepsin with a transition-state analogue. The objective is to define the positions of the protons at the active site by refinement using the neutron data. In line with work on serine proteinases, where neutron diffraction has provided some of the most definitive data on the catalytic mechanism, it is expected that this work will have a major significance for studies of the aspartic proteinase enzymes.

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Citation

Cooper, J.B. and Myles, D.A.A. (2000) A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin Acta Crystallographica Section D: Biological Crystallography, D56, (2), pp. 246-248. (doi:10.1107/S0907444900000603).

More information

Published date: February 2000
Keywords: neutron diffraction, endothiapepsin, laue diffraction, aspartic proteinases

Identifiers

Local EPrints ID: 56789
URI: http://eprints.soton.ac.uk/id/eprint/56789
ISSN: 0907-4449
PURE UUID: 3d61f44a-c5a5-44c1-baec-36de15341c69

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Date deposited: 22 Aug 2008
Last modified: 17 Jul 2017 14:30

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Contributors

Author: J.B. Cooper
Author: D.A.A. Myles

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