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Structural studies of proteins by high-flux X-ray and neutron solution scattering.

Physical studies on biomolecules are of importance in that quantitative measurements of macromolecular structure and dynamics will provide a more rigorous understanding of the functional roles of these macromolecules. Protein crystallography (which uses diffraction phenomena) is the most powerful technique since three-dimensional models to atomic resolution are obtained (Blundell & Johnson, 1976). In a number of situations, it is essential to complement the crystallographic investigation by the use of low resolution structural methods, such as solution scattering. Solution scattering experiments are also based on diffraction properties, but the macromolecules are now viewed in random orientations. In solution scattering, a solution of the sample is irradiated by a highly collimated beam of X-rays or neutrons (see Fig. 7 below). The intensity of the scattering