ArticleProteins2019
Cryo-electron microscopy targets in CASP13: Overview and evaluation of results.
Article in Proteins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Cryo-EM Analysis in CASP16.Proteins · 2026Article
- CASP15 cryo-EM protein and RNA targets: Refinement and analysis using experimental maps.Proteins · 2023Article
- Breaking the conformational ensemble barrier: Ensemble structure modeling challenges in CASP15.Proteins · 2023Article
- Application of Homology Modeling by Enhanced Profile-Profile Alignment and Flexible-Fitting Simulation to Cryo-EM Based Structure Determination.International journal of molecular sciences · 2022Article
- Atomic model validation using the CCP-EM software suite.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- Continuous Automated Model EvaluatiOn (CAMEO)-Perspectives on the future of fully automated evaluation of structure prediction methods.Proteins · 2021Article
- Cryo-EM targets in CASP14.Proteins · 2021Article
- Computational models in the service of X-ray and cryo-electron microscopy structure determination.Proteins · 2021Article
- Assessment of protein-protein interfaces in cryo-EM derived assemblies.Nature communications · 2021Article
- Cryo-EM model validation recommendations based on outcomes of the 2019 EMDataResource challenge.Nature methods · 2021Article
- TEMPy2: a Python library with improved 3D electron microscopy density-fitting and validation workflows.Acta crystallographica. Section D, Structural biology · 2021Article
- Automated Modeling and Validation of Protein Complexes in Cryo-EM Maps.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Homology modeling in the time of collective and artificial intelligence.Computational and structural biotechnology journal · 2020Review
- Article
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Authors and funding
7 authors.
Funding
Abstract
Structures of seven CASP13 targets were determined using cryo-electron microscopy (cryo-EM) technique with resolution between 3.0 and 4.0 Å. We provide an overview of the experimentally derived structures and describe results of the numerical evaluation of the submitted models. The evaluation is carried out by comparing coordinates of models to those of reference structures (CASP-style evaluation), as well as checking goodness-of-fit of modeled structures to the cryo-EM density maps. The performance of contributing research groups in the CASP-style evaluation is measured in terms of backbone accuracy, all-atom local geometry and similarity of inter-subunit interfaces. The results on the cryo-EM targets are compared with those on the whole set of eighty CASP13 targets. A posteriori refinement of the best models in their corresponding cryo-EM density maps resulted in structures that are very close to the reference structure, including some regions with better fit to the density.
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