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Peer-reviewedCC BYIUCrJ

Cryo-EM: the revolution continues

4 affiliations
  1. 1Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada
  2. 2Department of Biochemistry, Goethe University, Frankfurt am Main, Germany
  3. 3Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt 60438, Germany
  4. 4MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom

Abstract

The near-universal adoption of electron cryo-microscopy (cryo-EM) by structural and cell biologists has led to exponential growth of the field, especially over the last two decades, with a doubling in the number of deposited electron-microscopy density maps every 2.5 years. This exponential growth has changed in recent years to become linear. Cryo-EM methods are now able to contribute to our structural understanding of biological complexity ranging from atomic resolution maps of assemblies of multiprotein complexes to in situ investigation of protein structures in the context of intact cells, snapshots of multiple conformations and insights into fundamental chemical mechanisms underlying biological function. Combined with dramatic advances in artificial intelligence, the increasing democratization and implementation of cryo-EM appears poised to drive a new revolution in digital biology.

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BibTeX
@article{subramaniam2026cryoem,
  title = {{Cryo-EM: the revolution continues}},
  author = {Sriram Subramaniam and Werner Kühlbrandt and Richard Henderson},
  journal = {IUCrJ},
  year = {2026},
  month = may,
  doi = {10.1107/s2052252526003842},
  url = {https://doi.org/10.1107/s2052252526003842},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Cryo-EM: the revolution continues
AU  - Sriram Subramaniam
AU  - Werner Kühlbrandt
AU  - Richard Henderson
PY  - 2026
DA  - 2026/05/20
JO  - IUCrJ
DO  - 10.1107/s2052252526003842
UR  - https://doi.org/10.1107/s2052252526003842
AB  - The near-universal adoption of electron cryo-microscopy (cryo-EM) by structural and cell biologists has led to exponential growth of the field, especially over the last two decades, with a doubling in the number of deposited electron-microscopy density maps every 2.5 years. This exponential growth has changed in recent years to become linear. Cryo-EM methods are now able to contribute to our structural understanding of biological complexity ranging from atomic resolution maps of assemblies of multiprotein complexes to in situ investigation of protein structures in the context of intact cells, snapshots of multiple conformations and insights into fundamental chemical mechanisms underlying biological function. Combined with dramatic advances in artificial intelligence, the increasing democratization and implementation of cryo-EM appears poised to drive a new revolution in digital biology.
SN  - 2052-2525
ER  -