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X-ray crystallography is a technique in crystallography in which the pattern produced by the diffraction of x-rays through the closely spaced lattice of atoms in a crystal is recorded and then analyzed to
reveal the nature of that lattice.
The material and molecular structure of a substance can often be inferred by quantitative study of this pattern. It is widely
used in chemistry and biochemistry to determine the structures of molecules, including DNA and
proteins. The first protein structure was of myoglobin, as determined by Max Perutz and Sir John Cowdery Kendrew in 1958, which led to a Nobel Prize in Chemistry. X-ray crystallography played a
major role in elucidating the double-helix structure of DNA. See Rosalind Franklin, James D. Watson, Francis Crick. Today X-ray
crystallography is often used to determine how drugs, such as anti-cancer medications, can be improved to better influence their
protein targets.
To determine a structure, the substance must first be crystallized. This can be a painstaking procedure for macromolecules such as DNA. Then the crystals are harvested and often frozen with
liquid nitrogen. Freezing crystals both reduces radiation damage incurred during
data collection and decreases thermal motion within the crystal. Crystals are placed on a diffractometer, a machine that emits
a beam of x-rays. The x-rays diffract off the electrons in the crystal, and the
pattern of diffraction is recorded on film and scanned into a computer.
The molecule must be crystallized because one photon diffracted by one electron
cannot be reliably detected. However, because of the regular crystalline structure, the photons are diffracted by corresponding
electrons in many symmetrically arranged molecules. Because waves of the same frequency whose peaks match reinforce each other,
the signal becomes detectable.
Through a Fourier transform the measured data is moved from
reciprocal space to real
space. The resulting complex equation describes the electron density within the unit
cell of a crystal. The X-ray crystallographer must then interpret this map to determine the connectivities of atoms within
the molecule of interest. Once a model of a protein's structure has been determined, it is deposited in the Protein Databank .
See also:
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