Abstract
Illuminating the secrets of crystals: microcrystal electron diffraction in structural biology
Highlights
Rob Barringer*X-ray crystallography (XRC) has visualised biological macromolecules in exquisite detail for over 50 years, relying on a combination of mathematical principles to offer insight into atomic structures
Life is dependent on the ability of cells to perform a myriad of functions alone or in communities as tissues
Proteins act as nano-scale cellular ‘tools’ with functions that are intimately linked to their unique structure; the role that protein architecture plays in biomolecular interactions has a long history, most commonly typified in the mind of the public by the ‘lock-and-key’ hypothesis (Koshland, 1994)
Summary
X-ray crystallography (XRC) has visualised biological macromolecules in exquisite detail for over 50 years, relying on a combination of mathematical principles to offer insight into atomic structures. Crystals can diffract various electromagnetic waves aside from the conventional X-ray, offering an alternative approach to crystallographic structural analysis. Microcrystal electron diffraction (MicroED) illuminates crystals with electron waves instead of X-rays. Two specialised groups have demonstrated that MicroED can give high-resolution (often atomic) data, and appears to be developing into a powerful alternative method to XRC or electron microscopy of macromolecules. How MicroED compares to XRC will be key to assessing it as a stand-alone crystallographic technique. This review presents a critical analysis of MicroED, with comments on theoretical and practical aspects and suggestions of further work and development
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