Powder diffractionPowder diffraction is a scientific technique using X-ray, neutron, or electron diffraction on powder or microcrystalline samples for structural characterization of materials. An instrument dedicated to performing such powder measurements is called a powder diffractometer. Powder diffraction stands in contrast to single crystal diffraction techniques, which work best with a single, well-ordered crystal. Diffraction grating The most common type of powder diffraction is with x-rays, the focus of this article although some aspects of neutron powder diffraction are mentioned.
X-ray absorption spectroscopyX-ray absorption spectroscopy (XAS) is a widely used technique for determining the local geometric and/or electronic structure of matter. The experiment is usually performed at synchrotron radiation facilities, which provide intense and tunable X-ray beams. Samples can be in the gas phase, solutions, or solids. XAS data is obtained by tuning the photon energy, using a crystalline monochromator, to a range where core electrons can be excited (0.1-100 keV).
X-ray spectroscopyX-ray spectroscopy is a general term for several spectroscopic techniques for characterization of materials by using x-ray radiation. When an electron from the inner shell of an atom is excited by the energy of a photon, it moves to a higher energy level. When it returns to the low energy level, the energy which it previously gained by the excitation is emitted as a photon which has a wavelength that is characteristic for the element (there could be several characteristic wavelengths per element).
Structure factorIn condensed matter physics and crystallography, the static structure factor (or structure factor for short) is a mathematical description of how a material scatters incident radiation. The structure factor is a critical tool in the interpretation of scattering patterns (interference patterns) obtained in X-ray, electron and neutron diffraction experiments. Confusingly, there are two different mathematical expressions in use, both called 'structure factor'.
X-ray crystallographyX-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.
Absorption spectroscopyAbsorption spectroscopy refers to spectroscopic techniques that measure the absorption of electromagnetic radiation, as a function of frequency or wavelength, due to its interaction with a sample. The sample absorbs energy, i.e., photons, from the radiating field. The intensity of the absorption varies as a function of frequency, and this variation is the absorption spectrum. Absorption spectroscopy is performed across the electromagnetic spectrum.
Crystallographic databaseA crystallographic database is a database specifically designed to store information about the structure of molecules and crystals. Crystals are solids having, in all three dimensions of space, a regularly repeating arrangement of atoms, ions, or molecules. They are characterized by symmetry, morphology, and directionally dependent physical properties. A crystal structure describes the arrangement of atoms, ions, or molecules in a crystal.
Scherrer equationThe 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. It is used in the determination of size of crystals in the form of powder.
Structural bioinformaticsStructural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds and local motifs, principles of molecular folding, evolution, binding interactions, and structure/function relationships, working both from experimentally solved structures and from computational models.
Structural alignmentStructural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions.
