Abstract
The recent technological advances in electron microscopes, detectors, as well as image processing and reconstruction software have brought single particle cryo-electron microscopy (cryo-EM) into prominence for determining structures of bio-molecules at near atomic resolution. This has been particularly true for virus capsids, ribosomes, and other large assemblies, which have been the ideal specimens for structural studies by cryo-EM approaches. An analysis of time series metadata of virus structures on the methods of structure determination, resolution of the structures, and size of the virus particles revealed a rapid increase in the virus structures determined by cryo-EM at near atomic resolution since 2010. In addition, the data highlight the median resolution (∼3.0 Å) and size (∼310.0 Å in diameter) of the virus particles determined by X-ray crystallography while no such limits exist for cryo-EM structures, which have a median diameter of 508 Å. Notably, cryo-EM virus structures in the last four years have a median resolution of 3.9 Å. Taken together with minimal sample requirements, not needing diffraction quality crystals, and being able to achieve similar resolutions of the crystal structures makes cryo-EM the method of choice for current and future virus capsid structure determinations.
Original language | English (US) |
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Pages (from-to) | 1-4 |
Number of pages | 4 |
Journal | Journal of Structural Biology |
Volume | 201 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2018 |
Externally published | Yes |
Bibliographical note
Funding Information:This work is partly supported by the bridge funding from the Department of Integrative Structural and Computational Biology at The Scripps Research Institute , La Jolla, CA 92037.
Publisher Copyright:
© 2017 Elsevier Inc.
Keywords
- Capsid structure
- Cryo-electron microscopy
- Cryo-EM
- Virus structure
- X-ray crystallography