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Breaking the next Cryo-EM resolution barrier – Atomic resolution determination of proteins!

Ka Man Yip, Niels Fischer, Elham Paknia, Ashwin Chari, Holger Stark
doi: https://doi.org/10.1101/2020.05.21.106740
Ka Man Yip
Department of Structural Dynamics, MPI for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany
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Niels Fischer
Department of Structural Dynamics, MPI for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany
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Elham Paknia
Department of Structural Dynamics, MPI for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany
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Ashwin Chari
Department of Structural Dynamics, MPI for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany
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Holger Stark
Department of Structural Dynamics, MPI for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany
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  • For correspondence: hstark1@gwdg.de
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Summary

Single particle cryo-EM is a powerful method to solve the three-dimensional structures of biological macromolecules. The technological development of electron microscopes, detectors, automated procedures in combination with user friendly image processing software and ever-increasing computational power have made cryo-EM a successful and largely expanding technology over the last decade. At resolutions better than 4 Å, atomic model building starts becoming possible but the direct visualization of true atomic positions in protein structure determination requires significantly higher (< 1.5 Å) resolution, which so far could not be attained by cryo-EM. The direct visualization of atom positions is essential for understanding protein-catalyzed chemical reaction mechanisms and to study drug-binding and -interference with protein function. Here we report a 1.25 Å resolution structure of apoferritin obtained by cryo-EM with a newly developed electron microscope providing unprecedented structural details. Our apoferritin structure has almost twice the 3D information content of the current world record reconstruction (at 1.54 Å resolution 1). For the first time in cryo-EM we can visualize individual atoms in a protein, see density for hydrogen atoms and single atom chemical modifications. Beyond the nominal improvement in resolution we can also show a significant improvement in quality of the cryo-EM density map which is highly relevant for using cryo-EM in structure-based drug design.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
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Posted May 22, 2020.
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Breaking the next Cryo-EM resolution barrier – Atomic resolution determination of proteins!
Ka Man Yip, Niels Fischer, Elham Paknia, Ashwin Chari, Holger Stark
bioRxiv 2020.05.21.106740; doi: https://doi.org/10.1101/2020.05.21.106740
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Breaking the next Cryo-EM resolution barrier – Atomic resolution determination of proteins!
Ka Man Yip, Niels Fischer, Elham Paknia, Ashwin Chari, Holger Stark
bioRxiv 2020.05.21.106740; doi: https://doi.org/10.1101/2020.05.21.106740

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