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A powder X-ray diffractometer in motion. X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract in specific directions.
The resulting map of the directions of the X-rays far from the sample is called a diffraction pattern. It is different from X-ray crystallography which exploits X-ray diffraction to determine the arrangement of atoms in materials, and also has other components such as ways to map from experimental diffraction measurements to the positions of atoms.
These developed into the two main branches of crystallography, X-ray crystallography and electron diffraction. The quality and throughput of solving crystal structures greatly improved in the second half of the 20th century, with the developments of customized instruments and phasing algorithms.
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.
Inelastically scattered X-rays have intermediate phases and so in principle are not useful for X-ray crystallography. In practice X-rays with small energy transfers are included with the diffraction spots due to elastic scattering, and X-rays with large energy transfers contribute to the background noise in the diffraction pattern.
Pages in category "X-ray crystallography" ... Energy-dispersive X-ray diffraction; X-ray crystallography; X-ray diffraction; A. Anomalous X-ray scattering; B. Bernal ...