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  2. Structure factor - Wikipedia

    en.wikipedia.org/wiki/Structure_factor

    In 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 ...

  3. X-ray crystallography - Wikipedia

    en.wikipedia.org/wiki/X-ray_crystallography

    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.

  4. Rietveld refinement - Wikipedia

    en.wikipedia.org/wiki/Rietveld_refinement

    The neutron and X-ray diffraction of powder samples results in a pattern characterised by reflections (peaks in intensity) at certain positions. The height, width and position of these reflections can be used to determine many aspects of the material's structure.

  5. X-ray scattering techniques - Wikipedia

    en.wikipedia.org/wiki/X-ray_scattering_techniques

    This is an X-ray diffraction pattern formed when X-rays are focused on a crystalline material, in this case a protein. Each dot, called a reflection, forms from the coherent interference of scattered X-rays passing through the crystal.

  6. R-factor (crystallography) - Wikipedia

    en.wikipedia.org/wiki/R-factor_(crystallography)

    In the Cambridge Structural Database of small-molecule structures, more than 95% of the 500,000+ crystals have an R-factor lower than 0.15, and 9.5% have an R-factor lower than 0.03. Crystallographers also use the Free R-Factor ( R F r e e {\displaystyle R_{Free}} ) [ 3 ] to assess possible overmodeling of the data.

  7. Scherrer equation - Wikipedia

    en.wikipedia.org/wiki/Scherrer_Equation

    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.

  8. Bragg's law - Wikipedia

    en.wikipedia.org/wiki/Bragg's_law

    Typical diffraction patterns, for instance the Figure, show spots for different directions (plane waves) of the electrons leaving a crystal. 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 ...

  9. Le Bail method - Wikipedia

    en.wikipedia.org/wiki/Le_Bail_method

    The refinement process continues by setting the new calculated structure factor to the observed structure factor value. The process is then repeated with the new structure factor estimate. At this point, the unit cell, background, peak widths, peak shape, and resolution function are refined, and the parameters are improved.