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. 16.1, p. 345   | 1 | 2 |

Section 16.1.9.3. Integration with multiple-beam diffraction

G. M. Sheldrick,c H. A. Hauptman,b C. M. Weeks,b* R. Millerb and I. Usóna

a Institut für Anorganisch Chemie, Universität Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany,bHauptman–Woodward Medical Research Institute, Inc., 73 High Street, Buffalo, NY 14203-1196, USA, and cLehrstuhl für Strukturchemie, Universität Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany
Correspondence e-mail:  weeks@orion.hwi.buffalo.edu

16.1.9.3. Integration with multiple-beam diffraction

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Recent experimental work in the field of multiple-beam diffraction provides grounds for hope that a generally applicable solution to the problem of obtaining individual invariant values can be found. It has been shown that triplet invariants can be measured for lysozyme with a mean error of approximately 20° (Weckert et al., 1993[link]; Weckert & Hümmer, 1997[link]). In addition, direct methods strengthened by simulated triplet invariants have been used to redetermine the structure of BPTI at resolutions as low as 2.0 Å (Mathiesen & Mo, 1997[link], 1998[link]). Currently, the one-at-a-time methods used to measure triplet phases seriously limit practical applications, but faster methods of data collection have been proposed (Shen, 1998[link]). If the means can, in fact, be found for measuring significant numbers of triplet phases quickly and accurately, dual-space direct methods may become routinely applicable to much lower resolution data than is currently possible.

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