The accuracy of protein models automatically built into cryo-EM maps with ARP/wARP
Open Access
- 26 January 2021
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta crystallographica. Section D, Structural biology
- Vol. 77 (2), 142-150
- https://doi.org/10.1107/s2059798320016332
Abstract
Recent developments in cryogenic electron microscopy (cryo-EM) have enabled structural studies of large macromolecular complexes at resolutions previously only attainable using macromolecular crystallography. Although a number of methods can already assist in de novo building of models into high-resolution cryo-EM maps, automated and reliable map interpretation remains a challenge. Presented here is a systematic study of the accuracy of models built into cryo-EM maps using ARP/wARP. It is demonstrated that the local resolution is a good indicator of map interpretability, and for the majority of the test cases ARP/wARP correctly builds 90% of main-chain fragments in regions where the local resolution is 4.0 Å or better. It is also demonstrated that the coordinate accuracy for models built into cryo-EM maps is comparable to that of X-ray crystallographic models at similar local cryo-EM and crystallographic resolutions. The model accuracy also correlates with the refined atomic displacement parameters.Keywords
Funding Information
- European Commission (H2020-EINFRA-2015-1-675858)
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