Ray collimation Definition and 2 Discussions

Small-angle X-ray scattering (SAXS) is a small-angle scattering technique by which nanoscale density differences in a sample can be quantified. This means that it can determine nanoparticle size distributions, resolve the size and shape of (monodisperse) macromolecules, determine pore sizes, characteristic distances of partially ordered materials, and much more. This is achieved by analyzing the elastic scattering behaviour of X-rays when travelling through the material, recording their scattering at small angles (typically 0.1 – 10°, hence the "Small-angle" in its name). It belongs to the family of small-angle scattering (SAS) techniques along with small-angle neutron scattering, and is typically done using hard X-rays with a wavelength of 0.07 – 0.2 nm.. Depending on the angular range in which a clear scattering signal can be recorded, SAXS is capable of delivering structural information of dimensions between 1 and 100 nm, and of repeat distances in partially ordered systems of up to 150 nm. USAXS (ultra-small angle X-ray scattering) can resolve even larger dimensions, as the smaller the recorded angle, the larger the object dimensions that are probed.
SAXS and USAXS belong to a family of X-ray scattering techniques that are used in the characterization of materials. In the case of biological macromolecules such as proteins, the advantage of SAXS over crystallography is that a crystalline sample is not needed. Furthermore, the properties of SAXS allow investigation of conformational diversity in these molecules. Nuclear magnetic resonance spectroscopy methods encounter problems with macromolecules of higher molecular mass (> 30–40 kDa). However, owing to the random orientation of dissolved or partially ordered molecules, the spatial averaging leads to a loss of information in SAXS compared to crystallography.

View More On Wikipedia.org