Unravelling biological macromolecules with cryo-electron microscopy

Abstract

Knowledge of the three-dimensional structures of proteins and other biological macromolecules often aids understanding of how they perform complicated tasks in the cell. Because many such tasks involve the cleavage or formation of chemical bonds, structural characterization at the atomic level is most useful. Developments in the electron microscopy of frozen hydrated samples (cryo-electron microscopy) are providing unprecedented opportunities for the structural characterization of biological macromolecules. This is resulting in a wave of information about processes in the cell that were impossible to characterize with existing techniques in structural biology.

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Figure 1: Growth in structural biology over the past 40 years.
Figure 2: Membrane protein structural biology.
Figure 3: Soluble macromolecular machines.
Figure 4: Image classification enables the study of macromolecular dynamics.

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Acknowledgements

We thank Y. Cheng, D. Barford and R. Henderson for comments on an early version of this manuscript. S.H.W.S is funded by the UK Medical Research Council (MC_UP_A025_1013).

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Correspondence to Sjors H. W. Scheres.

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Fernandez-Leiro, R., Scheres, S. Unravelling biological macromolecules with cryo-electron microscopy. Nature 537, 339–346 (2016). https://doi.org/10.1038/nature19948

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