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Published December 6, 2013 | Supplemental Material
Journal Article Open

4D Cryo-Electron Microscopy of Proteins


Cryo-electron microscopy is a form of transmission electron microscopy that has been used to determine the 3D structure of biological specimens in the hydrated state and with high resolution. We report the development of 4D cryo-electron microscopy by integrating the fourth dimension, time, into this powerful technique. From time-resolved diffraction of amyloid fibrils in a thin layer of vitrified water at cryogenic temperatures, we were able to detect picometer movements of protein molecules on a nanosecond time scale. Potential future applications of 4D cryo-electron microscopy are numerous, and some are discussed here.

Additional Information

© 2013 American Chemical Society. Received: November 11, 2013; Publication Date (Web): December 6, 2013. The authors declare no competing financial interest. This work was supported by the National Science Foundation and the Air Force Office of Scientific Research in the Physical Biology Center for Ultrafast Science and Technology (UST) supported by the Gordon and Betty Moore Foundation at Caltech. A.W.P.F. is supported by a Marie Curie International Outgoing Fellowship. We thank A. W. McDowall and the Beckman Institute for help with sample preparations and for useful discussions.

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