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Automated model building and protein identification in cryo-EM maps
Open accessPreprint — published as 10.1038/s41586-024-07215-4 · Paper page
Abstract
Interpreting electron cryo-microscopy (cryo-EM) maps with atomic models requires high levels of expertise and labour-intensive manual intervention. We present ModelAngelo, a machine-learning approach for automated atomic model building in cryo-EM maps. By combining information from the cryo-EM map with information from protein sequence and structure in a single graph neural network, ModelAngelo builds atomic models for proteins that are of similar quality as those generated by human experts. For nucleotides, ModelAngelo builds backbones with similar accuracy as humans. By using its predicted amino acid probabilities for each residue in hidden Markov model sequence searches, ModelAngelo outperforms human experts in the identification of proteins with unknown sequences. ModelAngelo will thus remove bottlenecks and increase objectivity in cryo-EM structure determination.
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Deep Residual Learning for Image Recognition
He, K., Zhang, X., Ren, S., & Sun, J. (2016) · 2016 IEEE Conference on Computer Vision and Pattern Recognition (CVPR) · doi:10.1109/cvpr.2016.90 · Cited by 235,474
Vaswani, A., Shazeer, N., Parmar, N., Uszkoreit, J., Jones, L., Gomez, A. N., Kaiser, L., & Polosukhin, I. (2017) · arXiv · doi:10.48550/arxiv.1706.03762 · Cited by 120,404
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Feature Pyramid Networks for Object Detection
Lin, T.-Y., Dollar, P., Girshick, R., He, K., Hariharan, B., & Belongie, S. (2017) · 2017 IEEE Conference on Computer Vision and Pattern Recognition (CVPR) · doi:10.1109/cvpr.2017.106 · Cited by 30,939
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Mfold web server for nucleic acid folding and hybridization prediction
Zuker, M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg595 · Cited by 13,404
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391
Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 7,953
Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850
Accelerated Profile HMM Searches
Eddy, S. R. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002195 · Cited by 6,975
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- 14. Lin, Z., et al. Language models of protein sequences at the scale of evolution enable accurate structure prediction. bioRxiv (2022). URL https://www.biorxiv.org/content/early/2022/07/21/2022.07.20.500902. https://www.biorxiv.org/content/early/2022/07/21/2022.07.20.500902.full.pdf.
- Jamali, K. , Kimanius, D. & Scheres, S. H . A graph neural network approach to automated model building in cryo-EM maps. In The Eleventh International Conference on Learning Representations (2023). URL https://openreview.net/forum?id=65XDF_nwI61.
- 2019, Macromolecular structure determination using x-rays, neutrons and electrons: recent developments in phenix, Acta Crystallographica Section D: Structural Biology, 75, 861, 10.1107/S2059798319011471 · DOI · Paper page
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Mallet, V., Rapisarda, C., Minoux, H., & Ovsjanikov, M. (2025) · Bioinformatics · doi:10.1093/bioinformatics/btaf157 · Cited by 2
Venette-Smith, N. L., Vishwakarma, R. K., Venkatakrishnan, V., Dollinger, R., Schultz, J., Babitzke, P., Anand, G. S., Gilmour, D. S., Armache, J., & Murakami, K. S. (2026) · Nature Communications · doi:10.1038/s41467-026-75963-0 · Cited by 2
Fenwick, C. W., Turelli, P., Duhoo, Y., Lau, K., Hérate, C., Marlin, R., Lamrayah, M., Campos, J., Esteves-Leuenberger, L., Farina, A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.18.549530 · Cited by 2
Structure of the human heparan-α-glucosaminide N-acetyltransferase (HGSNAT)Preprint
Navratna, V., Kumar, A., & Mosalaganti, S. (2024) · eLife · doi:10.7554/elife.93510.1 · Cited by 2
Keles, I., Manger, S., Roth, P., Scheffer, M. P., & Frangakis, A. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.05.611430 · Cited by 2
Genomic and structural insights into Jyvaskylavirus, the first giant virus isolated from FinlandPreprint
Almeida, G. M. D. F., Arriaga, I., de Azevedo, B. L., Leppänen, M., Abrahão, J. S., Andréani, J., Zabeo, D., Ravantti, J., Abrescia, N. G. A., & Sundberg, L. (2025) · eLife · doi:10.7554/elife.103492.2 · Cited by 2
Axonemal dynein contributions to flagellar beat types and waveformsPreprint
Fochler, S., Doran, M. H., Beneke, T., Smith, J., Fort, C., Walker, B. J., Brown, A., Gluenz, E., & Wheeler, R. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.06.687033 · Cited by 2
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Tortorici, M. A., Choi, A., Gibson, C. A., Lee, J., Brown, J. T., Stewart, C., Joshi, A., Harari, S., Willoughby, I., Treichel, C., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.25.607996 · Cited by 2
Perera, M., Tan, W., Yang, E., Jain, O., Aggarwal, M., Venugopal, H., Iskander, J., Berry, J. D., Leis, A. P., & Shakeel, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.23.700950 · Cited by 2
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Konstantoulea, K., Kunach, P., Tagad, H. D., Diamond, M. I., & Louros, N. N. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.29.727653 · Cited by 2
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Dubianok, Y., Kumar, A., & Rak, A. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4418-8_2 · Cited by 1
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Dai, M., Dong, Z.-E., Fu, W., Xu, K., & Zhang, Q. C. (2025) · Proceedings of the AAAI Conference on Artificial Intelligence · doi:10.1609/aaai.v39i1.31987 · Cited by 1
Zhang, Y., Zhong, S., Xu, S., Wang, Z., Xin, C., Ni, F., Yan, F., Lu, X., Sun, S., Wang, H., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147637 · Cited by 1
Lee, C. S., Grba, D. N., Wright, J. J., Ivanov, B. S., & Hirst, J. (2025) · Science Advances · doi:10.1126/sciadv.adz0693 · Cited by 1
Cryogenic electron microscopy and tomography of ex vivo and in situ virus particles
Xu, L., & Chiu, W. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00018-4 · Cited by 1
Ho, A. W. S., Fukuzawa, T., Koga, H., Ohmine, K., Kawauchi, H., Muraoka, M., Ikuta, Y., Gupta, G., Okuda, M., Onami, I., et al. (2025) · EBioMedicine · doi:10.1016/j.ebiom.2025.106009 · Cited by 1
Xia, Y., Guo, Q., & Liu, T. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148947 · Cited by 1
Chen, J., Li, T., He, J., & Huang, S. (2025) · Structure · doi:10.1016/j.str.2025.11.004 · Cited by 1
Deep learning–based postprocessing and model building for cryo-electron microscopy maps
Li, T., & Huang, S. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103196 · Cited by 1
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Rasmussen, T., Küspert, J., Schönemann, L., Geiger, D., & Böttcher, B. (2025) · Communications Biology · doi:10.1038/s42003-025-09396-8 · Cited by 1
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Djabeur, N., Jeckelmann, J.-M., Ayoub, N., Harder, D., & Fotiadis, D. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169725 · Cited by 1
Melchers, J. M., Juraszek, J., Hulswit, R. J. G., van Overveld, D., Le, L., van Kuppeveld, F. J. M., Hurdiss, D. L., Bosch, B., Langedijk, J. P. M., & Bakkers, M. J. G. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1013998 · Cited by 1
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Oki, H., Takebe, K., Bonsu, A. O., Fujii, K. K., Masuda, R., Henderson, N., Mima, T., Koide, T., Moradi, M., Matsushita, O., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71099-3 · Cited by 2
Protein language models for structural biology
Xiang, C., Cheng, B., Peng, Z., & Yang, J. (2026) · Nature Computational Science · doi:10.1038/s43588-026-00993-z · Cited by 1
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Zhang, T., Liu, Z., Ma, Y., Feng, C., & Han, R. (2026) · Bioinformatics · doi:10.1093/bioinformatics/btag350 · Cited by 1
Guzmán-Solís, A. A., Ouizougun-Oubari, M., Escaffre, O., Larsen, B. B., Lopez, M., Locklear, S., Kumar, M., Juelich, T. L., Smith, J. K., Zhang, L., et al. (2026) · Science Translational Medicine · doi:10.1126/scitranslmed.adw8573 · Cited by 1
Metadata
- Authors
- Jamali, K., Käll, L., Zhang, R., Brown, A., Kimanius, D., & Scheres, S. H. W.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Science for Life Laboratory (SE)
- Washington University in St. Louis (US)
- Harvard University (US)
- Corresponding author
- Jamali, Kiarash
- Kimanius, Dari
- Scheres, Sjors H.W.
- Venue
- Nature
- Publisher
- openRxiv
- Published
- 2023-05-16
- Volume
- 628
- Issue
- 8007
- Pages
- 450-457
- ISSN
- 0028-0836 (ISSN-L)
- PMC
- PMC11006616
- OpenAlex
- W4392155415
- Cited by
- 686
- References
- 72
- Citations by year
- 2026: 259 · 2025: 264 · 2024: 134 · 2023: 28
- FWCI
- 120.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Nature (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Apollo (University of Cambridge) (acceptedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, cc-by)
- Funders
- European Commission (HORIZON2020, 895412)
- Knut och Alice Wallenbergs Stiftelse (2022.0032)
- National Institutes of Health
- Medical Research Council (MC_UP_A025_1013)
- National Institute of General Medical Sciences (R01GM138854, R01GM141109)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- cryo-EM density maps, protein identification, graph neural networks, protein structure determination, machine learning
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