Anomalous X-ray scattering
Anomalous X-ray scattering (AXRS or XRAS) is a non-destructive determination technique within
Atomic scattering factors
In X-ray diffraction the scattering factor f for an atom is roughly proportional to the number of electrons that it possesses. However, for wavelengths that approximate those for which the atom strongly absorbs radiation the scattering factor undergoes a change due to anomalous dispersion. The dispersion not only affects the magnitude of the factor but also imparts a phase shift in the elastic collision of the photon. The scattering factor can therefore best be described as a complex number[1]
- f = fo + Δf' + i.Δf"
Contrast variation
The anomalous aspects of X-ray scattering have become the focus of considerable interest in the scientific community because of the availability of
Protein crystallography
In protein crystallography, anomalous scattering refers to a change in a diffracting X-ray's phase that is unique from the rest of the atoms in a crystal due to strong X-ray absorbance.[2] The amount of energy that individual atoms absorb depends on their atomic number. The relatively light atoms found in proteins such as carbon, nitrogen, and oxygen do not contribute to anomalous scattering at normal X-ray wavelengths used for X-ray crystallography.[3] Thus, in order to observe anomalous scattering, a heavy atom must be native to the protein or a heavy atom derivative should be made. In addition, the X-ray's wavelength should be close to the heavy atom's absorption edge.
List of methods
- Multi-wavelength anomalous diffraction (MAD)
- Single-wavelength anomalous diffraction (SAD)
- Diffraction anomalous fine structure (DAFS) combines the use of anomalous diffraction with X-ray absorption fine structure (XAFS).[4]
References
- ISBN 0-486-68011-8original publication 1963
- ^ Glusker J.P. et al. (1994). Crystal structure analysis for chemists and biologists. Wiley-VCH
- ^ Rhodes, G. (2000). Crystallography made crystal clear (2nd ed.). San Diego: Academic Press.
- PMID 25343791.
External links
- X-ray Anomalous Scattering at skuld.bmsc.washington.edu. A resource mainly aimed at crystallographers.
- PHENIX glossary, describes the techniques supported by the commonly-used PHENIX refining program, including MAD & SAD.