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X-Ray Crystallography

In x-ray crystallography, X-rays are diffracted through the closely-spaced lattice of atoms in a crystal. The pattern produced can be analyzed to reveal the nature of the lattice. This technique is used commonly in both chemistry and biochemistry to determine structures of molecules such as DNA, proteins, and complex inorganic compounds. Single crystals of a material are generally used in x-ray crystallography, but if crystals are not available microcrystalline powdered samples can be substituted in a much more complex process.

Examples of substances examined using x-ray crystallography in single-crystal methods include fullerenes, metalloporphyrins, and other complex compounds. It is also commonly used in the pharmaceutical industry. The primary problem in single-crystal methods is getting a good-quality crystal to examine.

In powder diffraction methods, it's much easier to prepare the sample, but the information thus gained can be limited and more difficult to interpret.

The first protein crystal structure examined with x-ray crystallography was sperm whale myoglobin, leading to a Nobel Prize in chemistry for Max Perutz and Sir John Cowdery Kendrew. It was inspired by the observation of myoglobin crystals forming in pools of blood on whaling ship decks.

Web Resources On X-Ray Crystallography

X-ray Crystallography
X-ray Crystallography and Protein Structure Determination

Book Resources On X-Ray Crystallography

An Introduction to X-ray Crystallography by Michael M. Woolfson
Structure Determination by X-Ray Crystallography by Ladd & Palmer

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