Abstract
Cryoelectron microscopy (cryo-EM) combined with three-dimensional image reconstruction techniques allows researchers to view macromolecular structures at resolutions below 10 Å. Cryo-EM has thus become an alternative method for solving the structure of biomolecules that remain beyond the reach of nuclear magnetic resonance (NMR) or x-ray crystallographic methods. Cryo-EM is an improvement over these methods in other ways as well. NMR is limited by the size of the molecule that can be studied (30 kD or less) and by the solubility of the molecule in question. X-ray crystallography is limited by the ability to make crystals that diffract appropriately. Cryo-EM does not suffer from these limitations and, in addition, offers a view of the hydrated conformation of biological molecules. The method has been extremely useful, for example, in the elucidation of the structure of whole viruses.
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