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EDITORIAL
Method of the Year 2015
The end of blob-ology: single-particle cryo-electron microscopy (cryo-EM) is now being used to solve macromolecular structures at high resolution.
npg 201 6 Nature America, Inc. All rights reserved.
The three-dimensional structure of a protein or protein complex provides crucial insights into its biological function. As a structure-determination technique, cryo-EM has played second fiddle to the higher- resolution approaches of X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. This is rapidly changing, however, thanks to recent technical advances that now allow near-atomic-resolution structures to be solved using cryo-EM. The time is right to celebrate single-particle cryo-EM as our Method of the Year.
For decades, X-ray crystallography has been the go-to approach for solving protein structures. However, many proteinsespecially membrane proteins and protein complexesare stubbornly difficult, if not impossible, to crystallize. Alternatives to traditional crystallography have had different limitations. For example, the technique of serial femtosecond crystallography, carried out using an X-ray free-electron laser (XFEL), requires a slew of easier-to-produce microcrystals rather than single large protein crystals, but the competition for beamtime at a highly specialized...