Electron diffraction of microcrystals is a new powerful tool of cryo-electron microscopy, which makes it possible to determine the structure of three-dimensional crystals from a rotation series of diffraction patterns. Unlike X-ray crystallography, this method allows one to study micro- and even nanosized crystals. In this case, it is sufficient to have one or several crystals to obtain the structure with a high spatial resolution, which significantly reduces the necessary sample volume. The methodological aspects of application of electron diffraction of microcrystals are considered on the example of classical model protein: lysozyme.
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