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X-ray diffraction is a generic term for phenomena associated with changes in the direction of X-ray beams due to interactions with the electrons around atoms. It occurs due to elastic scattering , when there is no change in the energy of the waves.
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 and characteristic distances of partially ordered materials. [1]
Small-angle scattering is particularly useful because of the dramatic increase in forward scattering that occurs at phase transitions, known as critical opalescence, and because many materials, substances and biological systems possess interesting and complex features in their structure, which match the useful length scale ranges that these techniques probe.
X-ray reflectivity is an analytical technique for determining thickness, roughness, and density of single layer and multilayer thin films. Wide-angle X-ray scattering (WAXS), a technique concentrating on scattering angles 2θ larger than 5°. Spectrum of various inelastic scattering processes that can be probed with inelastic X-ray scattering ...
It is an X-ray-diffraction [2] method and commonly used to determine a range of information about crystalline materials. The term WAXS is commonly used in polymer sciences to differentiate it from SAXS but many scientists doing "WAXS" would describe the measurements as Bragg/X-ray/powder diffraction or crystallography.
Compared with destructive techniques, e.g. three-dimensional electron backscatter diffraction (3D EBSD), [5] with which the sample is serially sectioned and imaged, 3DXRD and similar X-ray nondestructive techniques have the following advantages: They require less sample preparation, thus limiting the introduction of new structures in the sample.
An X-ray diffraction pattern of a crystallized enzyme. The pattern of spots (reflections) and the relative strength of each spot (intensities) can be used to determine the structure of the enzyme. The relative intensities of the reflections provides information to determine the arrangement of molecules within the crystal in atomic detail.