P. R. Moore
Daresbury Laboratory
7 Papers
154 Citations
P. R. Moore is an academic researcher from Daresbury Laboratory. The author has contributed to research in topics: Synchrotron Radiation Source & Wiggler. The author has an hindex of 6, co-authored 7 publications. Previous affiliations of P. R. Moore include Birkbeck, University of London.
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Papers
Facilities for solution scattering and fibre diffraction at the Daresbury SRS
Colin Nave,John R. Helliwell,P. R. Moore,A. W. Thompson,J. S. Worgan,R. J. Greenall,A. M. Miller,S. K. Burley,J. Bradshaw,W. J. Pigram,Watson Fuller,D. P. Siddons,M. Deutsch,R. T. Tragear +13 more
TL;DR: The small-angle scattering facility at Daresbury has been constructed for diffraction studies of a wide range of naturally occurring and synthetic materials The high brightness of the SRS is combined with focusing optics, resulting in exposure times that can be two or three orders of magnitude less than those required on a conventional source as mentioned in this paper.
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Instrumentation for glancing angle x‐ray absorption spectroscopy on the Synchrotron Radiation Source
Stefania Pizzini,Kevin J. Roberts,G.N. Greaves,N. Harris,P. R. Moore,E. Pantos,Richard J. Oldman +6 more
TL;DR: A versatile instrument for glancingangle x-ray absorption spectroscopy (XAS) and xray reflectivity in routine use on the Daresbury Synchrotron Radiation Source is described in this paper.
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The wiggler protein crystallography workstation at the Daresbury SRS: Progress and results
John R. Helliwell,John R. Helliwell,Miroslav Z. Papiz,Miroslav Z. Papiz,I.D. Glover,J. Habash,J. Habash,A.W. Thompson,A.W. Thompson,P. R. Moore,P. R. Moore,N. Harris,N. Harris,D. Croft,D. Croft,E. Pantos,E. Pantos +16 more
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Central data collection facility for protein crystallography, small angle diffraction and scattering at the Daresbury Laboratory Synchrotron Radiation Source (SRS), England
John R. Helliwell,Trevor J. Greenhough,P.D. Carr,S.A. Rule,P. R. Moore,Andrew Thompson,J. S. Worgan +6 more
TL;DR: In this paper, an experimental workstation for protein crystallography using synchrotron X-radiation is described, where different modes of the single, bent, triangular monochromator are discussed for both the rapid collection of high Bragg resolution native crystal data and high spectral resolution (( delta lambda / lambda )
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A new macromolecular crystallography Station (9.5) on the SRS wiggler beam line for very rapid Laue and rapidly tunable monochromatic measurements: Commissioning and first results
Andrew Thompson,J. Habash,S. J. Harrop,John R. Helliwell,Colin Nave,P.W. Atkinson,S. Samar Hasnain,I.D. Glover,P. R. Moore,N. Harris,S. H. Kinder,S. G. Buffey +11 more
TL;DR: The Station 9.5 at the Daresbury Synchrotron Radiation Source (SRS) as discussed by the authors has been used for macromolecular crystallography beyond what is provided for with Stations 7.2, 9.6 and 9.7 by providing a point focused white beam (from a Pt-coated toroid mirror) and/or a rapidly tunable monochromatic beam (using a water-cooled double-crystal monochromaator).
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