Definition
In a scattering experiment, a solution of macromolecules is exposed to X-rays (with wavelength λ typically around 0.15 nm) or thermal neutrons (λ≈0.5 nm). The scattered intensity I(s) is recorded as a function of momentum transfer s (s=4πsinθ/λ, where 2θ is the angle between the incident and scattered radiation). From the intensity of the solution the scattering from only the solvent is subtracted. The random positions and orientations of particles result in an isotropic intensity distribution which, for monodisperse non-interacting particles, is proportional to the scattering from a single particle averaged over all orientations. The net particle scattering is proportional to the squared difference in scattering length density (electron density for X-rays and nuclear/spin density for neutrons) between particle and solvent – the so-called contrast. The contrast can be varied in neutron scattering using H2O/D2O mixtures or selective deuteration to yield additional information. The information content of SAS data is illustrated here in the figure on the right, which shows X-ray scattering patterns from proteins with different folds and molecular masses. At low angles (2-3 nm resolution) the curves are rapidly decaying functions of s essentially determined by the particle shape, which clearly differ. At medium resolution (2 to 0.5 nm) the differences are already less pronounced and above 0.5 nm resolution all curves are very similar. SAS thus contains information about the gross structural features – shape, quaternary and tertiary structure – but is not suitable for the analysis of the atomic structure.
Read more about this topic: Biological Small-angle Scattering
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