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A powder X-ray diffractometer in motion. X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract in specific directions.
William Lawrence Bragg proposed a model in which the incoming X-rays are scattered specularly (mirror-like) from each plane; from that assumption, X-rays scattered from adjacent planes will combine constructively (constructive interference) when the angle θ between the plane and the X-ray results in a path-length difference that is an integer ...
Myoglobin sketch Alpha helix. 1958 – Myoglobin was the very first crystal structure of a protein molecule. [2] Myoglobin cradles an iron-containing heme group that reversibly binds oxygen for use in powering muscle fibers, and those first crystals were of myoglobin from the sperm whale, whose muscles need copious oxygen storage for deep dives.
The first X-ray diffraction experiment was conducted in 1912 by Max von Laue, [7] while electron diffraction was first realized in 1927 in the Davisson–Germer experiment [8] and parallel work by George Paget Thomson and Alexander Reid. [9] These developed into the two main branches of crystallography, X-ray crystallography and electron ...
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X-ray optics is the branch of optics dealing with X-rays, rather than visible light.It deals with focusing and other ways of manipulating the X-ray beams for research techniques such as X-ray diffraction, X-ray crystallography, X-ray fluorescence, small-angle X-ray scattering, X-ray microscopy, X-ray phase-contrast imaging, and X-ray astronomy.
Other forms of elastic X-ray scattering besides single-crystal diffraction include powder diffraction, small-angle X-ray scattering and several types of X-ray fiber diffraction, which was used by Rosalind Franklin in determining the double-helix structure of DNA. In general, single-crystal X-ray diffraction offers more structural information ...
Isomorphous replacement (IR) is historically the most common approach to solving the phase problem in X-ray crystallography studies of proteins.For protein crystals this method is conducted by soaking the crystal of a sample to be analyzed with a heavy atom solution or co-crystallization with the heavy atom.