Cited by 59Advanced Electron Microscopy Techniques and ApplicationsProtein Structure and DynamicsEnzyme Structure and Function

Deep learning for reconstructing protein structures from cryo-EM density maps: Recent advances and future directions

Open access
Giri, Nabin, Roy, Raj S., Cheng, Jianlin·2023·Current Opinion in Structural Biology

Abstract

Cryo-Electron Microscopy (cryo-EM) has emerged as a key technology to determine the structure of proteins, particularly large protein complexes and assemblies in recent years. A key challenge in cryo-EM data analysis is to automatically reconstruct accurate protein structures from cryo-EM density maps. In this review, we briefly overview various deep learning methods for building protein structures from cryo-EM density maps, analyze their impact, and discuss the challenges of preparing high-quality data sets for training deep learning models. Looking into the future, more advanced deep learning models of effectively integrating cryo-EM data with other sources of complementary data such as protein sequences and AlphaFold-predicted structures need to be developed to further advance the field.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.sbi.2023.102536

Cites

53 of 55 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 3

  1. [17]He Jiahua, and Huang Sheng-You. ” EMNUSS: a deep learning framework for secondary structure annotation in cryo-EM maps.” Briefings in bioinformatics 22, no. 6 (2021): bbab156. 33954706 PMC8574626
  2. Jamali Kiarash, Kimanius Dari, and Scheres Sjors. ” ModelAngelo: Automated Model Building in Cryo-EM Maps.” arXiv preprint arXiv:2210.00006 (2022). · arXiv
  3. Fuchs Fabian, Worrall Daniel, Fischer Volker, and Welling Max. ” Se (3)-transformers: 3d roto-translation equivariant attention networks.” Advances in Neural Information Processing Systems 33 (2020): 1970– 1981. SE(3)-Transformer, a variant of the self-attention module for 3D point clouds, which is equivariant under continuous 3D roto-translations.

Cited by

Sorted by citations

Authors
Giri, N., Roy, R. S., & Cheng, J.
Affiliations
University of Missouri (US)
Corresponding author
Cheng, Jianlin
Venue
Current Opinion in Structural Biology
Publisher
Elsevier BV
Published
2023-04
Volume
79
Pages
102536
ISSN
0959-440X (ISSN-L)
OpenAlex
W4319723617
Cited by
59
References
55
Citations by year
2026: 9 · 2025: 20 · 2024: 17 · 2023: 13
FWCI
1.89
Type
journal article
Language
en
Open access
Locations
  • Current Opinion in Structural Biology (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • arXiv (Cornell University) (submittedVersion, cc-by-nc-sa)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • arXiv (Cornell University)
Funders
  • National Science Foundation (DBI1759934, IIS1763246)
  • U.S. Department of Energy (DE\u2013SC0021303, DE\u2013SC0020400, DE\u2013AR0001213)
  • National Institutes of Health (R01GM093123, R01GM146340)
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
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
cryo-EM density maps, protein structure reconstruction, deep learning, protein structure prediction, protein complexes, training data quality, AlphaFold, protein sequences, multi-source data fusion
MeSH terms
Deep Learning, Amino Acid Sequence, Models, Molecular, Protein Conformation, Proteins, Cryoelectron Microscopy

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review