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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. 14.1, p. 297
Section 14.1.9. Anomalous scattering without isomorphous replacement
aInstitute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, University of Oregon, Eugene, OR 97403, USA |
The treatment outlined above of phase determination by anomalous scattering assumed that data were available for a parent crystal devoid of anomalous scatters and an anomalously scattering isomorphous heavy-atom derivative. It is not uncommon that the native protein itself contains atoms which scatter anomalously or has been engineered to contain such scatterers. In such cases, measurements will usually be made at multiple wavelengths in order to exploit MAD phasing (Hendrickson, 1991![[link]](/graphics/greenarr.gif)
). If, however, measurements are available only at a single wavelength, they can be utilized to obtain some phase information (e.g. Matthews, 1970).
References
Hendrickson, W. A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science, 254, 51–58.Google Scholar
Matthews, B. W. (1970). Determination and refinement of phases for proteins. In Crystallographic computing, edited by F. R. Ahmed, S. R. Hall & C. P. Huber, pp. 146–159. Copenhagen: Munksgaard.Google Scholar
