Abstract
Crystal structure refinement using the new release of the Shelx program is discussed with emphasis on the incorporation of chemical information via constraints and restraints. It would be desirable to use refinement techniques in the structure solution as well, so as to incorporate chemical information into the phasing process. One such approach that looks very promising is Arp.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Sheldrick, G.M. and Schneider, T.R. (in press) Shelxl: Hign-resolution refinement, in C.W. Carter and R.M. Sweet (eds.), Methods in Enzymology, Academic Press, New York.
Parkinson, G., Voitechovsky, J., Clowney, L., Brünger, A.T., and Berman, H.M. (1996) New parameters for the refinement of nucleic acid-containing structures, Acta Cryst. D52, 57–64.
Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement, Acta Cryst. A47, 392–400.
Hendrickson, W.A. (1985) Stereochemically restrained refinement of macromolecular structures, in H.W. Wyckoff, C.H.W. Hirs and S.G. Timasheff (eds.), Methods in Enzymology, Academic Press, New York, Vol. 115B, pp. 252–270.
Driessen, H., Haneef, M.I.J., Harris, G.W., Howlin, B., Khan, G., and Moss, D.S. (1989) Restrain: Restrained structure-factor least-squares refinement program for macromolecular structures, J. Appl Cryst. 22, 510–516.
Rollett, J.S. (1970) Least-squares procedures in crystal structure analysis, in F.R. Ahmed, S.R. Hall and C.P. Huber (eds.), Computing in Crystallography, Munksgaard, Copenhagen, pp. 167–181.
Didisheim, J.J. and Schwarzenbach D. (1987) Rigid-link constraints and rigid-body molecules, Acta Cryst. A43, 226–232.
Gros, P., van Gunsteren, W.F., and Hoi, W.G. (1990) Inclusion of thermal motion in crystallographic Structures by restrained molecular dynamics, Science, 249, 1149–1152.
Clarage, Ib. and Phillips, G.N. (1994) Cross-validation tests of time-averaged molecular dynamics refinements for determination of protein structures by X-ray crystallography, Acta Cryst. D50, 24–36.
Brünger, A.T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, 355, 472–475.
Moews, P.C. and Kretsinger, R.H. (1975) Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis, J. Mol. Biol. 91, 201–228.
Tronrud, D.E., Ten Eyck, L.F., and Matthews, B.W. (1987) An efficient general-purpose least-squares refinement program for macromolecules, A eta Cryst. A43, 489–501.
Lamzin, V.S. and Wilson, K.S. (1993) Automated refinement of protein models, Acta Cryst. D49, 129–147.
Laskowski, R.A, MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) Procheck: a program to check the stereochemical quality of protein structures, J. Appl. Cryst. 26, 283–291.
Cruickshank, D.W.J. (1994) Protein precision re-examined: Luzzati plots do not estimate final errors, Poster Abstract, I.U.Cr. Meeting, Seattle.
Perrakis A, Sixma, T.A, Wilson, K.S., and Lamzin, V.S.(1997) The world according to wArp: improvement and extension of crystallographic phases, CCP4 Meeting, York, January 1997.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Sheldrick, G.M. (1998). Crystal Structure Refinement Incorporating Chemical Information. In: Fortier, S. (eds) Direct Methods for Solving Macromolecular Structures. NATO ASI Series, vol 507. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9093-8_12
Download citation
DOI: https://doi.org/10.1007/978-94-015-9093-8_12
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-4994-0
Online ISBN: 978-94-015-9093-8
eBook Packages: Springer Book Archive