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"A Review of High-Energy X-Ray Diffraction from Glasses and Liquids". ISRN Materials Science. 2012: 1– 19. doi: 10.5402/2012/852905. Eberhard Haug; Werner Nakel (2004). The elementary process of Bremsstrahlung. World Scientific Lecture Notes in Physics. Vol. 73. River Edge, NJ: World Scientific. ISBN 978-981-238-578-9.
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.
SADP of a single austenite crystal in a piece of steel. Selected area (electron) diffraction (abbreviated as SAD or SAED) is a crystallographic experimental technique typically performed using a transmission electron microscope (TEM).
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.
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.
In crystallography, the R-factor (sometimes called residual factor or reliability factor or the R-value or R Work) is a measure of the disagreement between the crystallographic model and the experimental X-ray diffraction data - lower the R value lower is the disagreement or better is the agreement.
Surface X-ray diffraction (SXRD), which is similar to RHEED but uses X-rays, and is also used to interrogate surface structure. [ 3 ] X-ray standing waves , another X-ray variant where the intensity decay into a sample from diffraction is used to analyze chemistry.
This is an X-ray diffraction pattern formed when X-rays are focused on a crystalline material, in this case a protein. Each dot, called a reflection, forms from the coherent interference of scattered X-rays passing through the crystal.