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

Fitzpatrick, A., Lorenz, U., Vanacore, G., Zewail, A. (2013). 4D cryo-electron microscopy of proteins. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 135(51), 19123-19126 [10.1021/ja4115055].

4D cryo-electron microscopy of proteins

Vanacore, G;
2013

Abstract

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
Articolo in rivista - Articolo scientifico
Ultrafast Electron Microscopy; Ultrafast Electron Diffraction; cryo-Electron Microscopy; amyloid proteins; protein dynamics
English
2013
135
51
19123
19126
none
Fitzpatrick, A., Lorenz, U., Vanacore, G., Zewail, A. (2013). 4D cryo-electron microscopy of proteins. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 135(51), 19123-19126 [10.1021/ja4115055].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/253507
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