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The angles that Bragg's law predicts are still approximately right, but in general there is a lattice of spots which are close to projections of the reciprocal lattice that is at right angles to the direction of the electron beam. (In contrast, Bragg's law predicts that only one or perhaps two would be present, not simultaneously tens to hundreds.)
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.
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.
Diffraction from a large three-dimensional periodic structure such as many thousands of atoms in a crystal is called Bragg diffraction. It is similar to what occurs when waves are scattered from a diffraction grating. Bragg diffraction is a consequence of interference between waves reflecting from many different crystal planes.
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 .
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 common feature of monochromators is the maintenance of a symmetrical geometry between the sample, the crystal and the detector. In this geometry the Bragg diffraction condition is obtained. The X-ray emission lines are very narrow (see figure 2), so the angles must be defined with considerable precision. This is achieved in two ways:
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.