Macromolecular Crystallography: Why Proteins are Not Like Small Molecules

-Bill Weis, Stanford University

The use of x-ray diffraction for the solution of macromolecular crystal structures differs from small molecules and materials at almost every stage of the process: sample preparation, data collection, phase determination, and refinement of the structure. An overview of protein crystallography will be presented, emphasizing these methodological differences. The use of synchrotron radiation in macromolecular crystallography will be discussed,including the importance of very bright monochromatic radiation for weakly diffracting crystals and tunable sources for multiwavelength anomalous dispersion (MAD) phasing.

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