Evidence map›Paper›PMID 38951555›Full record

ArticleNature communications2024

De novo atomic protein structure modeling for cryoEM density maps using 3D transformer and HMM.

Nabin Giri, Jianlin Cheng

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. CryoAtom improves model building for cryo-EM.Nature structural & molecular biology · 2026
    Article
  5. EMProt improves structure determination from cryo-EM maps.Nature structural & molecular biology · 2026
    Article
  6. Review
  7. Article
  8. Recognizing amino acid sidechains in a medium-resolution cryo-electron density map.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. A Labeled Dataset for AI-based Cryo-EM Map Enhancement.bioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. Review
  16. Review
  17. A labeled dataset for AI-based cryo-EM map enhancement.Computational and structural biotechnology journal · 2025
    Article
  18. Review
  19. Article
  20. CryoTEN: Efficiently Enhancing Cryo-EM Density Maps Using Transformers.bioRxiv : the preprint server for biology · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Nabin GiriDepartment of Electrical Engineering and Computer Science, University of Missouri, Columbia, MO, USA.ORCID 0000-0002-0251-3956
Jianlin ChengDepartment of Electrical Engineering and Computer Science, University of Missouri, Columbia, MO, USA. chengji@missouri.edu.ORCID 0000-0003-0305-2853

Funding

Deep learning methods for automated and accurate reconstruction of protein structures from cryo-EM image dataR01GM146340 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI CHENG, JIANLIN · 2022 to 2025
$1.4M
NIGMS NIH HHS R01 GM146340U.S. Department of Health & Human Services | NIH | Center for Information Technology (Center for Information Technology, National Institutes of Health) R01GM146340
6 · The paper itself

Abstract

Accurately building 3D atomic structures from cryo-EM density maps is a crucial step in cryo-EM-based protein structure determination. Converting density maps into 3D atomic structures for proteins lacking accurate homologous or predicted structures as templates remains a significant challenge. Here, we introduce Cryo2Struct, a fully automated de novo cryo-EM structure modeling method. Cryo2Struct utilizes a 3D transformer to identify atoms and amino acid types in cryo-EM density maps, followed by an innovative Hidden Markov Model (HMM) to connect predicted atoms and build protein backbone structures. Cryo2Struct produces substantially more accurate and complete protein structural models than the widely used ab initio method Phenix. Additionally, its performance in building atomic structural models is robust against changes in the resolution of density maps and the size of protein structures.

Indexed as

Cryoelectron MicroscopyMarkov ChainsModels, MolecularProtein ConformationProteinsAlgorithmsSoftwareProteins

Identifiers

PMID38951555
PMCPMC11217428

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.