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X-ray crystallography |
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X-ray crystallography, the study of crystal structures through X-ray diffraction techniques. When an X-ray beam bombards a crystalline lattice in a given orientation, the beam is scattered in a definite manner characterized by the atomic structure of the lattice. This phenomenon, known as X-ray diffraction, occurs when the wavelength of X-rays and the interatomic distances in the lattice have the same order of magnitude. In 1912, the German scientist Max von Laue predicted that crystals exhibit diffraction qualities. Concurrently, W. Friedrich and P. Knipping created the first photographic diffraction patterns. A year later Lawrence Bragg successfully analyzed the crystalline structures of potassium chloride and sodium chloride using X-ray crystallography, and developed a rudimentary treatment for X-ray/crystal interaction (Bragg's Law). Bragg's research provided a method to determine a number of simple crystal structures for the next 50 years. In the 1960s, the capabilities of X-ray crystallography were greatly improved by the incorporation of computer technology. Modern X-ray crystallography provides the most powerful and accurate method for determining single-crystal structures. Structures containing 100–200 atoms now can be analyzed on the order of 1–2 days, whereas before the 1960s a 20-atom structure required 1–2 years for analysis. Through X-ray crystallography the chemical structure of thousands of organic, inorganic, organometallic, and biological compounds are determined every year.
BibliographySee M. Buerger, X-Ray Crystallography (1980). |
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| The answer lies in the development of x-ray crystallography more than a century later in 1912. Advances in X-ray crystallography, which the team used to image the enzyme, were also critical. Table 1 is derived from the table of 44 reduced forms published originally in the International Tables for X-Ray Crystallography (1) and later, with revisions, in the Journal of Research of NIST (2). |
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