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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.
XAS is an interdisciplinary technique and its unique properties, as compared to x-ray diffraction, have been exploited for understanding the details of local structure in: glass, amorphous and liquid systems; solid solutions; doping and ionic implantation of materials for electronics; local distortions of crystal lattices; organometallic compounds
The structure factor is a critical tool in the interpretation of scattering patterns (interference patterns) obtained in X-ray, electron and neutron diffraction experiments. Confusingly, there are two different mathematical expressions in use, both called 'structure factor'.
To draw a pole figure, one chooses a particular crystal direction (e.g. the normal to the (100) plane) and then plots that direction, called a pole, for every crystal relative to a set of directions in the material. In a rolled metal, for example, the directions in the material are the rolling direction, transverse direction and rolling plane ...
Dr. Miller had done research on X-ray instrumentation at Washington University in St. Louis. Dr. Duffendack also hired Dr. Bill Parish, a well known researcher in X-ray diffraction, to head up the section of the lab on X-ray instrumental development. X-ray diffraction units were widely used in academic research departments to do crystal analysis.
X-ray crystal truncation rod scattering is a powerful method in surface science, based on analysis of surface X-ray diffraction (SXRD) patterns from a crystalline surface. For an infinite crystal, the diffracted pattern is concentrated in Dirac delta function like Bragg peaks.
The Scherrer equation, in X-ray diffraction and crystallography, is a formula that relates the size of sub-micrometre crystallites in a solid to the broadening of a peak in a diffraction pattern. It is often referred to, incorrectly, as a formula for particle size measurement or analysis.
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.