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Daresbury Laboratory

CRYSTAL98 Is the current version of the commercial HF program developed at the University of Torino and at Daresbury Laboratory (http //www.dl.ac.uk/TCS/Software/CRYSTAL/)... [Pg.2233]

CH would like to thank Daniel Bowron (CLRC, Rutherford Appleton Laboratory), Fred Mosselmanns (CLRC, Daresbury Laboratory), Will Pitner (The Queen s University of Belfast), Nick Terrill (CLRC, Daresbury Laboratory), and Philip Watson (University of Oregon) for contributing figures, as well as for useful discussions and comments in the preparation of this manuscript. [Pg.150]

N. Binsted, EXCURV98 CCLRC Daresbury Laboratory computer program, 1998. [Pg.151]

The financial support of the CICYT (project no. IN89-0066), DGICYT (project no. PB94-1529), and Consejerfa de Educacidn de la Comunidad de Madrid is gratefully thanked. We also acknowledge the support of NATO (grant CRG 920094) and the assistance of Dr. W. Bras and the Daresbury Laboratory (UK) in the synchrotron experiments. [Pg.397]

CCLRC Daresbury Laboratory, Warrington, Cheshire WA44AD, United Kingdom... [Pg.219]

Fig. 7. A typical X-ray diffraction pattern of the Fepr protein fromZJ. vulgaris (Hil-denborough). The pattern was recorded on station 9.6 at the Synchrotron Radiation Source at the CCLRC Daresbury Laboratory using a wavelength 0.87 A and a MAR-Research image-plate detector system with a crystal-to-detector distance of 220 nun. X-ray data clearly extend to a resolution of 1.5 A, or even higher. The crystal system is orthorhombic, spacegroup P2i2i2i with unit cell dimensions, a = 63.87, b = 65.01, c = 153.49 A. The unit cell contains four molecules of 60 kDa moleculEu- weight with a corresponding solvent content of approximately 48%. Fig. 7. A typical X-ray diffraction pattern of the Fepr protein fromZJ. vulgaris (Hil-denborough). The pattern was recorded on station 9.6 at the Synchrotron Radiation Source at the CCLRC Daresbury Laboratory using a wavelength 0.87 A and a MAR-Research image-plate detector system with a crystal-to-detector distance of 220 nun. X-ray data clearly extend to a resolution of 1.5 A, or even higher. The crystal system is orthorhombic, spacegroup P2i2i2i with unit cell dimensions, a = 63.87, b = 65.01, c = 153.49 A. The unit cell contains four molecules of 60 kDa moleculEu- weight with a corresponding solvent content of approximately 48%.
Fig. 4 Schematic representation of the detector arrangement on Station 16.4 of the SRS, Daresbury Laboratory, UK... Fig. 4 Schematic representation of the detector arrangement on Station 16.4 of the SRS, Daresbury Laboratory, UK...
Figure 10.1 (a) Distribution of emitted radiation from an electron travelling at relativistic speeds in a circular orbit, (b) The universal, vertically integrated, synchrotron radiation spectrum as a function of reduced wavelength. The axes are calibrated for the SRS at Daresbury Laboratory... [Pg.235]

Figure 10.5 Real-time image, with no computer processing, of magnetic domains and low-angle boundaries in iron-silicon taken using the Bede Scientific HI-RES detector at Daresbury Laboratory. The white radiation topograph was taken with X-rays of fundamental wavelength 1 A... Figure 10.5 Real-time image, with no computer processing, of magnetic domains and low-angle boundaries in iron-silicon taken using the Bede Scientific HI-RES detector at Daresbury Laboratory. The white radiation topograph was taken with X-rays of fundamental wavelength 1 A...
Kabsch, W. (1993a). Data collection and processing. In Sawyer, L., Issacs, N. and Bailey, S., eds. Proceedings of the CCP4 Study weekend. Daresbury laboratories, Warrington, UK, pp. 56-62. [Pg.74]

Bricogne, G. and Irwin, J. J. (1996). Proceedings of the CCP4 Study Weekend. Macromolecular Refinement, Dodson, E., Moore, M., Ralph A. and Bailey, S., eds, pp. 85-92. Warrington Daresbury Laboratory. [Pg.170]

CCP4 (1979). TheSERC (UK) Collaborative Computing Project No. 4, a Suite of Programs for Protein Crystallography. Daresbury Laboratory, Warrington, WA4 4AD, UK. [Pg.261]

S. C. Althorpe, P. Soldn, and G. G. Balint-Kurti, eds., Time-Dependent Quantum Dynamics CCP6 Collaborative Computational Project on Heavy Particle Dynamics (Daresbury Laboratory, Daresbury, Warrington, WA4 4AD, U.K., 2001). [Pg.299]

T.R. Forester and W. Smith, CCLRC, Daresbury Laboratory, Warrington, England, 1995. [Pg.101]

Def rtment of Crystallc raphy, Birkbeck College, Malet Street, London WCIE 7HX, England Science and Engineering Research Council, Daresbury Laboratory, Daresbury, Warrington, Cheshire WA4 4AD, En and... [Pg.31]

Synchrotron Radiation Source, SERC Daresbury Laboratory, Warrington WA4 4AD, Cheshire, U. K. [Pg.73]

Fig. 2. Layout of the Synchrotron Radiation Source (SRS) at the Daresbury Laboratory, U.K. Fig. 2. Layout of the Synchrotron Radiation Source (SRS) at the Daresbury Laboratory, U.K.
Advances in the techniques of EXAFS analysis pioneered at the Daresbury Laboratory have allowed the unfiltered EXAFS data to be simulated accurately and the observed differences can thus be interpreted structurally with some confidence. [Pg.86]

Knowles, P. F., Strange, R. W., Blackburn, N. J., Hasnain, S. S. ibid, (submitted, also available as Daresbury Laboratory report DL/SCI/P561E, 1987)... [Pg.93]

In the early years we had to depend on a relatively low-intensity x-ray source. High-resolution data was obtained through collaboration with John R. Helliwell and his group at the Daresbury Laboratory Synchrotron Radiation Source in England. Today greatly improved equipment and more synchrotron facilities are available for protein crystallography. [Pg.156]

SERC Daresbury Laboratory X-Ray Powder Users Group Meeting, September, 1983 and July 1985. [Pg.757]

Daresbury Laboratory Users Meeting, March 1981 and July 1985. [Pg.768]

C. S. Jeffery (ed.). Daresbury Laboratory Newsletter on Analysis of Astronomical Spectra, No 18. Dept, of Physics and Astron., Univ. of St. Andrews, Fife, Scotland, 1993. [Pg.419]


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