ArticleActa crystallographica. Section D, Structural biology2021
The accuracy of protein models automatically built into cryo-EM maps with ARP/wARP.
Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- gapTrick-structural characterization of protein-protein interactions using AlphaFold.Bioinformatics (Oxford, England) · 2025Article
- Outcomes of the EMDataResource cryo-EM Ligand Modeling Challenge.Nature methods · 2024Article
- DoubleHelix: nucleic acid sequence identification, assignment and validation tool for cryo-EM and crystal structure models.Nucleic acids research · 2023Article
- The CCP4 suite: integrative software for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2023Article
- Automatic and accurate ligand structure determination guided by cryo-electron microscopy maps.Nature communications · 2023Article
- Sequence-assignment validation in cryo-EM models with checkMySequence.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- Redeployment of automated MrBUMP search-model identification for map fitting in cryo-EM.Acta crystallographica. Section D, Structural biology · 2021Article
- Cryo-EM single-particle structure refinement and map calculation using Servalcat.Acta crystallographica. Section D, Structural biology · 2021Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
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.
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