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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 ...
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.
This means that X-rays are seemingly "reflected" off parallel crystal lattice planes perpendicular at the same angle as their angle of approach to the crystal with respect to the lattice planes; in the elastic light (typically X-ray)-crystal scattering, parallel crystal lattice planes perpendicular to a reciprocal lattice vector for the crystal ...
J. Als-Nielsen, D. McMorrow: Elements of Modern X-ray physics. Wiley, 2001 (chapter 5: diffraction by perfect crystals). 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.
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.
1908 - Bernhard Walter and Robert Wichard Pohl observed X-ray diffraction from a slit. [46] [47] 1912 - Max von Laue discovered diffraction patterns from crystals in an x-ray beam. [48] 1912 - Bragg diffraction, expressed through Bragg's law, is first presented by Lawrence Bragg on 11 November 1912 to the Cambridge Philosophical Society. [49]
In a wavelength-dispersive X-ray spectrometer, a single crystal diffracts the photons according to Bragg's law, which are then collected by a detector.By moving the diffraction crystal and detector relative to each other, a wide region of the spectrum can be observed.
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.