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Laue equation. In crystallography and solid state physics, the Laue equations relate incoming waves to outgoing waves in the process of elastic scattering, where the photon energy or light temporal frequency does not change upon scattering by a crystal lattice. They are named after physicist Max von Laue (1879–1960).
Free-electron lasers have been developed for use in X-ray diffraction and crystallography. [27] These are the brightest X-ray sources currently available; with the X-rays coming in femtosecond bursts. The intensity of the source is such that atomic resolution diffraction patterns can be resolved for crystals otherwise too small for collection.
Ray diagram of Von Laue formulation. In physics, a Bragg plane is a plane in reciprocal space which bisects a reciprocal lattice vector, , at right angles. [1] The Bragg plane is defined as part of the Von Laue condition for diffraction peaks in x-ray diffraction crystallography.
In many areas of science, Bragg's law, Wulff–Bragg's condition, or Laue–Bragg interference are a special case of Laue diffraction, giving the angles for coherent scattering of waves from a large crystal lattice. It describes how the superposition of wave fronts scattered by lattice planes leads to a strict relation between the wavelength ...
Unlike the kinematic theory of diffraction which describes the approximate position of Bragg or Laue diffraction peaks in reciprocal space, dynamical theory corrects for refraction, shape and width of the peaks, extinction and interference effects.
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.
After the discovery of x-rays by Wilhelm Röntgen in 1895, and of the principles of X-ray diffraction by Laue and the Bragg family, it took several decades for the benefits of diffraction imaging to be fully recognized, and the first useful experimental techniques to be developed. The first systematic reports of laboratory topography techniques ...
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.