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Qu'est-ce (qui) est X-ray motion analysis - définition
X-ray motion analysis
TECHNIQUE TO TRACK THE MOVEMENT OF OBJECTS USING X-RAYS
User:GaTech CNL X-Ray 01/sandbox; Draft:X-ray motion analysis
X-ray motion analysis is a technique used to track the movement of objects using X-rays. This is done by placing the subject to be imaged in the center of the X-ray beam and recording the motion using an image intensifier and a high-speed camera, allowing for high quality videos sampled many times per second.
X-ray spectroscopy
CHARACTERIZATION TECHNIQUE
Photon-in-photon-out; X-Ray Spectroscopy; X-ray spectrometry; X-ray spectra; X-Ray Absorption Edge Spectroscopy; X-Ray Absorption Fine Structure Spectroscopy; X-Ray Transmittance Spectroscopy; X-Ray Line Spectrum; X-ray spectrometer; Roentgen spectroscopy; X-ray spectrum; X-ray Spectrometry; Roentgen spectrometry; X-ray spectrograph; X-Ray Spectrometry
X-ray spectroscopy is a general term for several spectroscopic techniques for characterization of materials by using x-ray radiation.
X-ray crystallography
![Model of the arrangement of water molecules in ice, revealing the [[hydrogen bond]]s (1) that hold the solid together.](https://commons.wikimedia.org/wiki/Special:FilePath/3D model hydrogen bonds in water.svg?width=200 "Model of the arrangement of water molecules in ice, revealing the [[hydrogen bond]]s (1) that hold the solid together.")
![The incoming beam (coming from upper left) causes each scatterer to re-radiate a small portion of its intensity as a spherical wave. If scatterers are arranged symmetrically with a separation ''d'', these spherical waves will be in sync (add constructively) only in directions where their path-length difference 2''d'' sin θ equals an integer multiple of the [[wavelength]] λ. In that case, part of the incoming beam is deflected by an angle 2θ, producing a ''reflection'' spot in the [[diffraction pattern]].](https://commons.wikimedia.org/wiki/Special:FilePath/Bragg diffraction 2.svg?width=200 "The incoming beam (coming from upper left) causes each scatterer to re-radiate a small portion of its intensity as a spherical wave. If scatterers are arranged symmetrically with a separation ''d'', these spherical waves will be in sync (add constructively) only in directions where their path-length difference 2''d'' sin θ equals an integer multiple of the [[wavelength]] λ. In that case, part of the incoming beam is deflected by an angle 2θ, producing a ''reflection'' spot in the [[diffraction pattern]].")
![tetrahedrally]] and held together by single [[covalent bond]]s, making it strong in all directions. By contrast, graphite is composed of stacked sheets. Within the sheet, the bonding is covalent and has hexagonal symmetry, but there are no covalent bonds between the sheets, making graphite easy to cleave into flakes.](https://commons.wikimedia.org/wiki/Special:FilePath/Diamond and graphite2.jpg?width=200 "tetrahedrally]] and held together by single [[covalent bond]]s, making it strong in all directions. By contrast, graphite is composed of stacked sheets. Within the sheet, the bonding is covalent and has hexagonal symmetry, but there are no covalent bonds between the sheets, making graphite easy to cleave into flakes.")
![backbone]] from its N-terminus to its C-terminus.](https://commons.wikimedia.org/wiki/Special:FilePath/Myoglobin.png?width=200 "backbone]] from its N-terminus to its C-terminus.")
![Rocknest]]", October 17, 2012).<ref name="NASA-20121030" />](https://commons.wikimedia.org/wiki/Special:FilePath/PIA16217-MarsCuriosityRover-1stXRayView-20121017.jpg?width=200 "Rocknest]]\", October 17, 2012).<ref name=\"NASA-20121030\" />")
![A protein crystal seen under a [[microscope]]. Crystals used in X-ray crystallography may be smaller than a millimeter across.](https://commons.wikimedia.org/wiki/Special:FilePath/Protein crystal.jpg?width=200 "A protein crystal seen under a [[microscope]]. Crystals used in X-ray crystallography may be smaller than a millimeter across.")
TECHNIQUE USED FOR DETERMINING THE ATOMIC OR MOLECULAR STRUCTURE OF A CRYSTAL, IN WHICH THE ORDERED ATOMS CAUSE A BEAM OF INCIDENT X-RAYS TO DIFFRACT INTO SPECIFIC DIRECTIONS
X-ray structure; X-Ray Crystallography; X-Ray Diffraction Pattern; X ray diffraction; X-ray diffraction analysis; Crystallography, x-ray; Protein Crystallography; Protein crystallography; Xray crystallography; Xray Crystallography; X-ray Crystallography; X-ray crystalography; Crystallographic resolution; Laue diffraction; X-ray diffraction; History of X-ray crystallography; X ray crystallography; X-ray single-crystal analysis; X-ray crystal structure; Single-crystal X-ray crystallography; X-ray crystallographer; Laue method; X-ray diffraction crystallography; Single-crystal X-ray diffraction; X-ray structural analysis
X-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.
