A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin
A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin
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.
neutron diffraction, endothiapepsin, laue diffraction, aspartic proteinases
246-248
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Myles, D.A.A.
dee29ff3-3c05-4c17-8c4e-c418079f9b0f
February 2000
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Myles, D.A.A.
dee29ff3-3c05-4c17-8c4e-c418079f9b0f
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), .
(doi:10.1107/S0907444900000603).
Abstract
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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Published date: February 2000
Keywords:
neutron diffraction, endothiapepsin, laue diffraction, aspartic proteinases
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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: 15 Mar 2024 11:03
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Author:
J.B. Cooper
Author:
D.A.A. Myles
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