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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.
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. The resulting map of the directions of the X-rays far from the sample is called a diffraction pattern.
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. It is named after Paul Scherrer.
XRD may refer to: X-ray diffraction , used to study the structure, composition, and physical properties of materials Extensible Resource Descriptor , an XML format for discovery of metadata about a web resource
Small-angle X-ray scattering (SAXS) is a small-angle scattering technique by which nanoscale density differences in a sample can be quantified. This means that it can determine nanoparticle size distributions, resolve the size and shape of (monodisperse) macromolecules, determine pore sizes and characteristic distances of partially ordered materials. [1]
X-ray optics is the branch of optics dealing with X-rays, rather than visible light.It deals with focusing and other ways of manipulating the X-ray beams for research techniques such as X-ray diffraction, X-ray crystallography, X-ray fluorescence, small-angle X-ray scattering, X-ray microscopy, X-ray phase-contrast imaging, and X-ray astronomy.
The distance between these planes is called the d-spacing. The intensity of the d-space pattern is directly proportional to the number of electrons (atoms) in the imaginary planes. Every crystalline solid has a unique pattern of d-spacings (known as the powder pattern), which is a fingerprint for that solid.
In crystallography, the R-factor (sometimes called residual factor or reliability factor or the R-value or R Work) is a measure of the disagreement between the crystallographic model and the experimental X-ray diffraction data - lower the R value lower is the disagreement or better is the agreement.