Measurement of atom resolvability in cryo-EM maps with Q-scores
- Stanford Univ., CA (United States)
- SLAC National Accelerator Lab., Stanford Univ., Menlo Park, CA (United States)
- Stanford Univ., CA (United States); SLAC National Accelerator Lab., Stanford Univ., Menlo Park, CA (United States)
Cryogenic electron microscopy (cryo-EM) maps are now at the point where resolvability of individual atoms can be achieved. However, resolvability is not necessarily uniform throughout the map. We introduce a quantitative parameter to characterize the resolvability of individual atoms in cryo-EM maps, the map Q-score. Q-scores can be calculated for atoms in proteins, nucleic acids, water, ligands and other solvent atoms, using models fitted to or derived from cryo-EM maps. Q-scores can also be averaged to represent larger features such as entire residues and nucleotides. Averaged over entire models, Q-scores correlate very well with the estimated resolution of cryo-EM maps for both protein and RNA. Here, assuming the models they are calculated from are well fitted to the map, Q-scores can be used as a measure of resolvability in cryo-EM maps at various scales, from entire macromolecules down to individual atoms. Q-score analysis of multiple cryo-EM maps of the same proteins derived from different laboratories confirms the reproducibility of structural features from side chains down to water and ion atoms.
- Research Organization:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Organization:
- National Inst. of Health; USDOE Office of Science (SC)
- Grant/Contract Number:
- AC02-76SF00515
- OSTI ID:
- 1604578
- Journal Information:
- Nature Methods, Journal Name: Nature Methods Journal Issue: 3 Vol. 17; ISSN 1548-7091
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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