A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin

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), 246-248. (doi:10.1107/S0907444900000603).


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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.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1107/S0907444900000603
ISSNs: 0907-4449 (print)
Related URLs:
Keywords: neutron diffraction, endothiapepsin, laue diffraction, aspartic proteinases
Subjects: Q Science > Q Science (General)
Q Science > QK Botany
Q Science > QR Microbiology
Divisions : University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56789
Accepted Date and Publication Date:
February 2000Published
Date Deposited: 22 Aug 2008
Last Modified: 31 Mar 2016 12:37
URI: http://eprints.soton.ac.uk/id/eprint/56789

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