Abstract
When a beam of neutrons or X-rays encounters a protein in solution, a small portion of the beam will be deflected or “scattered.” The angular dependence of this scattering is related to the structure of the protein. For a solution of randomly oriented proteins, the scattering is concentrated in the vicinity of the direct beam, or zero-angle. Solution scattering is therefore often referred to as small-angle or low-angle scattering. Structural information encoded in the scattering data includes the overall size and shape of the protein. Although this information is relatively low-resolution, it is not limited by the requirement of having crystals and it can be applied to structures with dimensions in the range 10-1000 Å. This range is extremely useful for studies of proteins and the complexes they form.
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Trewhella, J., Krueger, J.K. (2002). Small-Angle Solution Scattering Reveals Information on Conformational Dynamics in Calcium-Binding Proteins and in their Interactions with Regulatory Targets. In: Vogel, H.J. (eds) Calcium-Binding Protein Protocols: Volume 2: Methods and Techniques. Methods in Molecular Biology™, vol 173. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-184-1:137
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DOI: https://doi.org/10.1385/1-59259-184-1:137
Publisher Name: Springer, Totowa, NJ
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