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  2. X-ray diffraction - Wikipedia

    en.wikipedia.org/wiki/X-ray_diffraction

    X-ray diffraction is a generic term for phenomena associated with changes in the direction of X-ray beams due to interactions with the electrons around atoms. It occurs due to elastic scattering , when there is no change in the energy of the waves.

  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. Structure factor - Wikipedia

    en.wikipedia.org/wiki/Structure_factor

    The amplitude and phase of this scattered wave will be the vector sum of the scattered waves from all the atoms () = = [1] [2] For an assembly of atoms, f j {\displaystyle f_{j}} is the atomic form factor of the j {\displaystyle j} -th atom.

  5. Resolution (structural biology) - Wikipedia

    en.wikipedia.org/wiki/Resolution_(structural...

    2.0 - 2.5: As 2.5 - 3.0, but number of sidechains in wrong rotamer is considerably less. Many small errors can normally be detected. Fold normally correct and number of errors in surface loops is small. Water molecules and small ligands become visible. 1.5 - 2.0: Few residues have wrong rotamer. Many small errors can normally be detected.

  6. Bragg's law - Wikipedia

    en.wikipedia.org/wiki/Bragg's_law

    The measurement of the angles can be used to determine crystal structure, see x-ray crystallography for more details. [ 5 ] [ 13 ] As a simple example, Bragg's law, as stated above, can be used to obtain the lattice spacing of a particular cubic system through the following relation:

  7. R-factor (crystallography) - Wikipedia

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

    In crystallography, the R-factor (sometimes called residual factor or reliability factor or the R-value or R Work) is a measure of the disagreement between the crystallographic model and the experimental X-ray diffraction data - lower the R value lower is the disagreement or better is the agreement.

  8. Powder diffraction - Wikipedia

    en.wikipedia.org/wiki/Powder_diffraction

    Powder X-ray diffraction (PXRD) operates under the assumption that the sample is randomly arranged. Therefore, a statistically significant number of each plane of the crystal structure will be in the proper orientation to diffract the X-rays. Therefore, each plane will be represented in the signal.

  9. Wavelength-dispersive X-ray spectroscopy - Wikipedia

    en.wikipedia.org/wiki/Wavelength-dispersive_X...

    [2] As the atomic number of the element increases so there are more possible electrons at different energy levels that can be ejected resulting in x-rays with different wavelengths. This creates spectra with multiple lines, one for each energy level. The largest peak in the spectrum is labelled K α, the next K β, and so on.