Berkeley Lab Research Review Winter 2000

ven a workhorse can't do everything. The dual advantages of high resolution and fast throughput make synchrotron-based x-ray crystallography, like that which is being carried out at Berkeley Lab's Advanced Light Source, the undisputed mainstay for solving protein structures. However, some 20 to 40 percent of all proteins are extremely difficult or even impossible to crystallize, including many found in the membranes which control the transportation of molecules and communication of signals across cell surfaces. This means that other technologies will also have critical roles to play. One alternative that does not require crystallized proteins is nuclear magnetic resonance (nmr) spectroscopy, a technology that exploits the spin of certain atomic nuclei to obtain structural, spatial, and even dynamic information about those nuclei. Conventional nmr spectroscopy, however, is essentially limited to the study of small proteins. For the study of macromolecular protein complexes, especially those that are difficult to coax into crystals, the best alternative to x-ray crystallography may be electron microscopy.
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