X-ray notation - ορισμός. Τι είναι το X-ray notation
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  3. X-ray notation

Τι (ποιος) είναι X-ray notation - ορισμός


X-ray notation         
X-ray notation is a method of labeling atomic orbitals that grew out of X-ray science. Also known as IUPAC notation, it was adopted by the International Union of Pure and Applied Chemistry in 1991 as a simplification of the older Siegbahn notation.
https://en.wikipedia.org/wiki/X-ray_notation
X-ray crystallography         
  • 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]].
  • Three methods of preparing crystals, A: Hanging drop. B: Sitting drop. C: Microdialysis
  • 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.
  • access-date=2018-11-28}}</ref> The electron density is obtained from experimental data, and the ligand is modeled into this electron density.
  • Structure of a protein alpha helix, with stick-figures for the covalent bonding within electron density for the crystal structure at ultra-high-resolution (0.91&nbsp;Å). The density contours are in gray, the helix backbone in white, sidechains in cyan, O atoms in red, N atoms in blue, and hydrogen bonds as green dotted lines.<ref>From PDB file 2NRL, residues 17–32.</ref>
  • Animation showing the five motions possible with a four-circle kappa goniometer. The rotations about each of the four angles φ, κ, ω and 2θ leave the crystal within the X-ray beam, but change the crystal orientation. The detector (red box) can be slid closer or further away from the crystal, allowing higher resolution data to be taken (if closer) or better discernment of the Bragg peaks (if further away).
  • backbone]] from its N-terminus to its C-terminus.
  • 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.
  • 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.
  • Workflow for solving the structure of a molecule by X-ray crystallography.
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.
https://en.wikipedia.org/wiki/X-ray_crystallography
X-ray crystallography         
  • 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]].
  • Three methods of preparing crystals, A: Hanging drop. B: Sitting drop. C: Microdialysis
  • 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.
  • access-date=2018-11-28}}</ref> The electron density is obtained from experimental data, and the ligand is modeled into this electron density.
  • Structure of a protein alpha helix, with stick-figures for the covalent bonding within electron density for the crystal structure at ultra-high-resolution (0.91&nbsp;Å). The density contours are in gray, the helix backbone in white, sidechains in cyan, O atoms in red, N atoms in blue, and hydrogen bonds as green dotted lines.<ref>From PDB file 2NRL, residues 17–32.</ref>
  • Animation showing the five motions possible with a four-circle kappa goniometer. The rotations about each of the four angles φ, κ, ω and 2θ leave the crystal within the X-ray beam, but change the crystal orientation. The detector (red box) can be slid closer or further away from the crystal, allowing higher resolution data to be taken (if closer) or better discernment of the Bragg peaks (if further away).
  • backbone]] from its N-terminus to its C-terminus.
  • 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.
  • 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.
  • Workflow for solving the structure of a molecule by X-ray crystallography.
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
¦ noun the study of crystals and their structure by means of the diffraction of X-rays by the regularly spaced atoms of crystalline materials.
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