Electron cryo-microscopy for elucidating the dynamic nature of live-protein complexes

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 2; p. 129436
• Main Author: Shigematsu, Hideki
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.02.2020
• Subjects: Classification; cryo-electron microscopy; crystallization; Dynamics; Electron cryo-microscopy; Heterogeneity; proteins; Single particle analysis; X-ray diffraction; Heterogeneity; Single particle analysis; Electron cryo-microscopy; Dynamics; Classification
• ISSN: 0304-4165; 1872-8006; 1872-8006
• DOI: 10.1016/j.bbagen.2019.129436

Recent innovations in the field of electron cryo-microscopy (cryo-EM) have achieved structure determination of target macromolecules at “near-atomic resolution”. In addition, cryo-EM has the potential to deal with proteins in multiple conformations in close to physiological conditions. This is an overview of the latest technical and methodological developments in cryo-EM, especially key features for elucidating the dynamic nature of specimens. It is now possible to elucidate “near-atomic resolution” structures by selecting “well-behaved” particles in Single Particle Analysis (SPA) of cryo-EM images. Currently, cryo-EM is utilized actively as an alternative to X-ray crystallography to obtain high-resolution structures of macromolecules, especially those which are hard to crystalize. One possible reason for difficulty in crystallization could be the dynamic nature of the specimen. New developments in the field of cryo-EM will make it possible to deal with specimen heterogeneity and reveal the dynamic nature of specimens. •An overview of key features for elucidating the dynamic nature of specimens in cryo-EM.•In current cryo-EM, “near-atomic resolution” can be achieved by selecting “well-behaved” images.•New algorithms in cryo-EM will reveal the dynamic nature of specimens.