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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.
Other forms of elastic X-ray scattering besides single-crystal diffraction include powder diffraction, small-angle X-ray scattering and several types of X-ray fiber diffraction, which was used by Rosalind Franklin in determining the double-helix structure of DNA. In general, single-crystal X-ray diffraction offers more structural information ...
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.
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 ...
The dynamical theory of diffraction considers the wave field in the periodic potential of the crystal and takes into account all multiple scattering effects. 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 ...
X-ray crystal truncation rod scattering is a powerful method in surface science, based on analysis of surface X-ray diffraction (SXRD) patterns from a crystalline surface. For an infinite crystal , the diffracted pattern is concentrated in Dirac delta function like Bragg peaks .
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