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Structure determination of low-molecular weight targets at near-atomic resolution using single-particle cryo-electron tomography

Published online by Cambridge University Press:  30 July 2021

Hsuan-Fu Liu ,
Ye Zhou ,
Xiaochen Du ,
Jonathan Bouvette ,
Mario Borgnia  and
Alberto Bartesaghi
Hsuan-Fu Liu
Affiliation:
Duke University, Durham, North Carolina, United States
Ye Zhou
Affiliation:
Duke University, North Carolina, United States
Xiaochen Du
Affiliation:
Duke University, United States
Jonathan Bouvette
Affiliation:
National Institute of Environmental Health Sciences, United States
Mario Borgnia
Affiliation:
National Institute of Environmental Health Sciences, United States
Alberto Bartesaghi
Affiliation:
Duke University, United States

Abstract

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Type
Cryo-electron Tomography: Present Capabilities and Future Potential
Information
Microscopy and Microanalysis , Volume 27 , Supplement S1 , August 2021 , pp. 3220 - 3222
Copyright
Copyright © The Author(s), 2021. Published by Cambridge University Press on behalf of the Microscopy Society of America

References

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Tegunov, D., Xue, L., Dienemann, C., Cramer, P., and Mahamid, J., “Multi-particle cryo-EM refinement with M visualizes ribosome-antibiotic complex at 3.5 Å in cells,” Nature Methods, vol. 18, no. 2, Art. no. 2, Feb. 2021.CrossRefGoogle Scholar
Bartesaghi, A., Lecumberry, F., Sapiro, G., and Subramaniam, S., “Protein Secondary Structure Determination by Constrained Single-Particle Cryo-Electron Tomography,” Structure, vol. 20, no. 12, pp. 2003–2013, Dec. 2012.CrossRefGoogle Scholar
Bouvette, J. et al. , “Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography,” bioRxiv, p. 2020.09.24.294983, Jan. 2021.Google ScholarPubMed