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In physics, the phase problem is the problem of loss of information concerning the phase that can occur when making a physical measurement. The name comes from the field of X-ray crystallography , where the phase problem has to be solved for the determination of a structure from diffraction data. [ 1 ]
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 ...
Crystals used in X-ray crystallography may be smaller than a millimeter across. Although crystallography can be used to characterize the disorder in an impure or irregular crystal, crystallography generally requires a pure crystal of high regularity to solve the structure of a complicated arrangement of atoms.
Anode X-ray sources have been successfully used to study gold (=) for example. [4] When doing X-ray measurements of a surface, the sample is held in Ultra-High Vacuum and the X-rays pass into and out of the UHV chamber through Beryllium windows. There are 2 approaches to chamber and diffractometer design that are in use.
Today, selenium-SAD is commonly used for experimental phasing due to the development of methods for selenomethionine incorporation into recombinant proteins. SAD is sometimes called "single-wavelength anomalous dispersion" , but no dispersive differences are used in this technique since the data are collected at a single wavelength.
X-ray diffraction computed tomography is an experimental technique that combines X-ray diffraction with the computed tomography data acquisition approach. X-ray diffraction (XRD) computed tomography (CT) was first introduced in 1987 by Harding et al. [1] using a laboratory diffractometer and a monochromatic X-ray pencil beam.
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.
To convert to an expression for crystal size in terms of the peak width in the scattering angle used in X-ray powder diffraction, we note that the scattering vector = (/) (/), where the here is the angle between the incident wavevector and the scattered wavevector, which is different from the in the scan.