Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron 
Microscopy

Khoshouei, Maryam; Danev, Radostin; Plitzko, Jürgen M.; Baumeister, Wolfgang

doi:10.1016/j.jmb.2017.07.004

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Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy

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Khoshouei, Maryam
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Danev, Radostin
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Plitzko, Jürgen M.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Baumeister, Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Khoshouei, M., Danev, R., Plitzko, J. M., & Baumeister, W. (2017). Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy. Journal of Molecular Biology (London), 429(17), 2611-2618. doi:10.1016/j.jmb.2017.07.004.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-E759-D

Abstract

Sixty years ago, the first protein structure of myoglobin was determined by John Kendrew and his colleagues; hemoglobin followed shortly thereafter. For quite some time, it seemed that only X-ray crystallography would be capable of determining the structure of proteins to high resolution. In recent years, cryo-electron microscopy has emerged as a viable alternative and indeed in many cases the preferred approach. It is capable of studying proteins that span a size range from several megadaltons to proteins as small as myoglobin and hemoglobin. (C) 2017 Elsevier Ltd. All rights reserved.