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International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 18.4, p. 396
Section 18.4.3.5. Computer power
a
National Cancer Institute, Brookhaven National Laboratory, Building 725A-X9, Upton, NY 11973, USA,bStructural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England, and CLRC, Daresbury Laboratory, Daresbury, Warrington, WA4 4AD, England, and cStructural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England |
There are no longer any restrictions on the full-matrix refinement of small-molecule crystal structures. However, the large size of the matrix, which increases as ![[N^{2}]](/teximages/bach1o3/bach1o3fi1441.svg)
, where N is the number of parameters, means that for macromolecules, which contain thousands of independent atoms, this approach is intractable with the computing resources normally available to the crystallographer. By extrapolating the progress in computing power experienced in recent years, it can be envisaged that the limitations will disappear during the next decade, as those for small structures have disappeared since the 1960s. Indeed, the advances in the speed of CPUs, computer memory and disk capacity continue to transform the field, which makes it hard to predict the optimal strategies for atomic resolution refinement, even over the next ten years.
