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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. It is named after Paul Scherrer.
This is the method used in the original discovery of X-ray diffraction. Laue scattering provides much structural information with only a short exposure to the X-ray beam, and is therefore used in structural studies of very rapid events (time resolved crystallography). However, it is not as well-suited as monochromatic scattering for determining ...
Screening for ovarian cancer is tricky because while CA-125 often does rise as ovarian tumors grow, there's not a single specific level that can tell a doctor a woman is at risk. Some women with ...
The use of computational methods for the powder X-ray diffraction data analysis is now generalized. It typically compares the experimental data to the simulated diffractogram of a model structure, taking into account the instrumental parameters, and refines the structural or microstructural parameters of the model using least squares based ...
Bragg diffraction (also referred to as the Bragg formulation of X-ray diffraction) was first proposed by Lawrence Bragg and his father, William Henry Bragg, in 1913 [1] after their discovery that crystalline solids produced surprising patterns of reflected X-rays (in contrast to those produced with, for instance, a liquid). They found that ...
In X-ray diffraction, the Rachinger correction is a method for accounting for the effect of an undesired K-alpha 2 peak in the energy spectrum. Ideally, diffraction measurements are made with X-rays of a single wavelength. Practically, the x-rays for a measurement are usually generated in an X-ray tube from a metal's K-alpha line. This ...
The units of the structure-factor amplitude depend on the incident radiation. For X-ray crystallography they are multiples of the unit of scattering by a single electron (2.82 m); for neutron scattering by atomic nuclei the unit of scattering length of m is commonly used.
Single-wavelength anomalous diffraction (SAD) is a technique used in X-ray crystallography that facilitates the determination of the structure of proteins or other biological macromolecules by allowing the solution of the phase problem.