ArticleActa crystallographica. Section D, Structural biology2021
Protein identification from electron cryomicroscopy maps by automated model building and side-chain matching.
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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Impurities in amyloid studies: The power of automated model building within a cautionary tale for structural biologists.Protein science : a publication of the Protein Society · 2025Article
- Recognizing amino acid sidechains in a medium-resolution cryo-electron density map.Protein science : a publication of the Protein Society · 2025Article
- Architecture of the baculovirus nucleocapsid revealed by cryo-EM.Nature communications · 2023Article
- Automated model building and protein identification in cryo-EM maps.bioRxiv : the preprint server for biology · 2023Article
- Improvement of cryo-EM maps by simultaneous local and non-local deep learning.Nature communications · 2023Article
- Molecular basis of stepwise cyclic tetra-adenylate cleavage by the type III CRISPR ring nuclease Crn1/Sso2081.Nucleic acids research · 2023Article
- Recent advances and current trends in cryo-electron microscopy.Current opinion in structural biology · 2022Review
- Cryo-EM structures of prion protein filaments from Gerstmann-Sträussler-Scheinker disease.Acta neuropathologica · 2022Article
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Authors and funding
7 authors.
Funding
Abstract
Using single-particle electron cryo-microscopy (cryo-EM), it is possible to obtain multiple reconstructions showing the 3D structures of proteins imaged as a mixture. Here, it is shown that automatic map interpretation based on such reconstructions can be used to create atomic models of proteins as well as to match the proteins to the correct sequences and thereby to identify them. This procedure was tested using two proteins previously identified from a mixture at resolutions of 3.2 Å, as well as using 91 deposited maps with resolutions between 2 and 4.5 Å. The approach is found to be highly effective for maps obtained at resolutions of 3.5 Å and better, and to have some utility at resolutions as low as 4 Å.
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