Λεπτομέρειες βιβλιογραφικής εγγραφής
| Τίτλος: |
Single-particle cryoEM: Theory and practice. |
| Συγγραφείς: |
Patwardhan A; Cellular Structure & 3D Bioimaging, European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), UK., Rosenthal PB; Structural Biology of Cells and Viruses Laboratory, The Francis Crick Institute, London, UK., Russo CJ; MRC Laboratory of Molecular Biology, Cambridge, UK., Henderson R; MRC Laboratory of Molecular Biology, Cambridge, UK. |
| Πηγή: |
Quarterly reviews of biophysics [Q Rev Biophys] 2026 Oct 15; Vol. 59, pp. e16. Date of Electronic Publication: 2026 Oct 15. |
| Τύπος έκδοσης: |
Journal Article; Review |
| Γλώσσα: |
English |
| Στοιχεία περιοδικού: |
Publisher: Cambridge Univ. Press Country of Publication: England NLM ID: 0144032 Publication Model: Electronic Cited Medium: Internet ISSN: 1469-8994 (Electronic) Linking ISSN: 00335835 NLM ISO Abbreviation: Q Rev Biophys Subsets: MEDLINE |
| Imprint Name(s): |
Original Publication: London, Cambridge Univ. Press. |
| Ιατρικοί όροι (MeSH): |
Cryoelectron Microscopy*/methods , Single Molecule Imaging*/methods |
| Περίληψη: |
Radiation damage is the fundamental limitation to the useful exposure in single-particle electron cryomicroscopy (cryoEM), so the goal of the field is to record near-perfect images, to extract as much information as possible from them, and then use this information to determine the three-dimensional structure of the desired biological molecule or molecular complex. This review presents a theoretical estimate of the number of single-particle images required to reach any desired resolution assuming perfect performance of all aspects of the imaging process. This target is then compared with the current state of cryoEM in practice, as represented by published structures in the Electron Microscopy Data Bank (EMDB). Considering recent structures, it becomes clear that the best structures in the 2.5-3.0 Å resolution range come within a factor of 3 of theoretical expectations. More typical datasets still require 100 times more images in practice than necessary in theory. This also applies to the higher resolution structures where larger datasets are essential. The reasons for this discrepancy are discussed alongside possible strategies to bring experimental structures closer to theoretical perfection. Finally, even the best cryoEM structures have significant radiation damage, which can only be ameliorated by recovering information from the best possible images at the beginning of the exposure at a fraction of the total dose currently used. |
| Grant Information: |
CC2106 United Kingdom CRUK_ Cancer Research UK; CC2106,MC_UP_120117 United Kingdom MRC_ Medical Research Council; CC2106 United Kingdom WT_ Wellcome Trust |
| Contributed Indexing: |
Keywords: B factor; Electron Microscopy Data Bank (EMDB); Protein Data Bank (PDB); cryogenic electron microscopy; radiation damage; single particle analysis; tomography |
| Entry Date(s): |
Date Created: 20261015 Date Completed: 20261015 Latest Revision: 20261015 |
| Update Code: |
20261015 |
| DOI: |
10.1017/S0033583526100249 |
| PMID: |
42876405 |
| Βάση Δεδομένων: |
MEDLINE |