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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.
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.
X-ray diffraction is a generic term for phenomena associated with changes in the direction of X-ray beams due to interactions with the electrons around atoms. It occurs due to elastic scattering , when there is no change in the energy of the waves.
André Authier: Dynamical theory of X-ray diffraction. IUCr monographs on crystallography, no. 11. Oxford University Press (1st edition 2001/ 2nd edition 2003). ISBN 0-19-852892-2. R. W. James: The Optical Principles of the Diffraction of X-rays. Bell., 1948. M. von Laue: Röntgenstrahlinterferenzen. Akademische Verlagsanstalt, 1960 (German).
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).
It is an X-ray-diffraction [2] method and commonly used to determine a range of information about crystalline materials. The term WAXS is commonly used in polymer sciences to differentiate it from SAXS but many scientists doing "WAXS" would describe the measurements as Bragg/X-ray/powder diffraction or crystallography .
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.
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.