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Electron crystallography



Electron crystallography is a method to determine the arrangement of atoms in solids using an electron microscope. It can complement X-ray crystallography on proteins, such as membrane proteins, that cannot easily form the large 3-dimensional crystals required for that process. Structures are usually determined from either 2-dimensional crystals (sheets or helices), polyhedrons such as viral capsids, or dispersed individual proteins. Electrons can be used in these situations, whereas X-rays cannot, because electrons interact more strongly with atoms than X-rays do. Thus, X-rays will travel through a thin 2-dimensional crystal without diffracting significantly, whereas electrons can be used to form an image. Conversely, the strong interaction between electrons and proteins makes thick (e.g. 3-dimensional) crystals impervious to electrons, which only penetrate short distances.

Additional recommended knowledge

One of the main difficulties in X-ray crystallography is determining phases in the diffraction pattern. Because no X-ray lens exists, X-rays cannot be used to form an image of the crystal being diffracted, and hence phase information is lost. Fortunately, electron microscopes contain electron lenses, and phase information tends to be much more reliable in electron crystallography.

A common problem to X-ray crystallography and electron crystallography is radiation damage, by which proteins are damaged as they are being imaged, limiting the resolution that can be obtained. This is especially troublesome in the setting of electron crystallography, where that radiation damage is focused on far fewer atoms. One technique used to limit radiation damage is electron cryomicroscopy, in which the samples undergo cryofixation and imaging takes place at liquid nitrogen or even liquid helium temperatures. Because of this problem, X-ray crystallography has been much more successful in determining the structure of proteins that are especially vulnerable to radiation damage.

The first electron crystallographic protein structure to achieve atomic resolution was bacteriorhodopsin, determined by Richard Henderson and coworkers at the Medical Research Council Laboratory of Molecular Biology in 1990. Since then, several other high-resolution structures have been determined by electron crystallography, including the light-harvesting complex, the nicotinic acetylcholine receptor, and the bacterial flagellum.

 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Electron_crystallography". A list of authors is available in Wikipedia.
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