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Journal Article

Current limitations to high-resolution structure determination by single-particle cryoEM

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D'Imprima,  Edoardo
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

D'Imprima, E., & Kühlbrandt, W. (2021). Current limitations to high-resolution structure determination by single-particle cryoEM. Quarterly Reviews of Biophysics, 54: e4. doi:10.1017/S0033583521000020.


Cite as: https://hdl.handle.net/21.11116/0000-0008-262D-C
Abstract
CryoEM has become the method of choice for determining the structure of large macromolecular complexes in multiple conformations, at resolutions where unambiguous atomic models can be built. Two effects that have limited progress in single-particle cryoEM are (i) beam-induced movement during image acquisition and (ii) protein adsorption and denaturation at the air-water interface during specimen preparation. While beam-induced movement now appears to have been resolved by all-gold specimen support grids with very small holes, surface effects at the air-water interface are a persistent problem. Strategies to overcome these effects include the use of alternative support films and new techniques for specimen deposition. We examine the future potential of recording perfect images of biological samples for routine structure determination at atomic resolution.