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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. R-factor (crystallography) - Wikipedia

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

    Small molecules (up to ca. 1000 atoms) usually form better-ordered crystals than large molecules, and thus it is possible to attain lower R-factors. 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.

  4. Patterson function - Wikipedia

    en.wikipedia.org/wiki/Patterson_function

    The Patterson function is used to solve the phase problem in X-ray crystallography.It was introduced in 1935 by Arthur Lindo Patterson while he was a visiting researcher in the laboratory of Bertram Eugene Warren at MIT.

  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. 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 ...

  7. 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.

  8. Debye–Waller factor - Wikipedia

    en.wikipedia.org/wiki/Debye–Waller_factor

    Now we see the overall structure factor may be represented as a weighted sum of structure factors () corresponding to each atom. Set the displacement between the location in space for which we would like to know the scattering density and the reference position for the nucleus equal to a new variable t → = x → − x → k 0 {\displaystyle ...

  9. Direct methods (electron microscopy) - Wikipedia

    en.wikipedia.org/wiki/Direct_methods_(electron...

    In electron diffraction, a diffraction pattern is produced by the interaction of the electron beam and the crystal potential. The real space and reciprocal space information about a crystal structure can be related through the Fourier transform relationships shown below, where () is in real space and corresponds to the crystal potential, and () is its Fourier transform in reciprocal space.