Evidence map›Paper›PMID 39433880›Full record

ArticleNature methods2024

DiffModeler: large macromolecular structure modeling for cryo-EM maps using a diffusion model.

Xiao Wang, Han Zhu, Genki Terashi, Manav Taluja, Daisuke Kihara

Abstract read
In one paragraph

Article in Nature methods, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Accurate Macromolecular Complex Modeling for Cryo-EM with CryoZeta.bioRxiv : the preprint server for biology · 2026
    Article
  4. CryoAtom improves model building for cryo-EM.Nature structural & molecular biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Finding antibodies in cryo-EM maps with CrAI.Bioinformatics (Oxford, England) · 2025
    Article
  18. Review
  19. AI-based methods for biomolecular structure modeling for Cryo-EM.Current opinion in structural biology · 2025
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Xiao WangDepartment of Computer Science, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0003-4435-7098
Han ZhuDepartment of Computer Science, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0009-0006-7408-8860
Genki TerashiDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0002-5339-909X
Manav TalujaDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0009-0005-1263-4224
Daisuke KiharaDepartment of Computer Science, Purdue University, West Lafayette, IN, USA. dkihara@purdue.edu.ORCID http://orcid.org/0000-0003-4091-6614

Funding

Building protein structure models for intermediate resolution cryo-electron microscopy mapsR01GM133840 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2020 to 2023
$1.6M
NIGMS NIH HHS R01 GM133840NSF | BIO | Division of Biological Infrastructure (DBI) DBI2003635NSF | BIO | Division of Molecular and Cellular Biosciences (MCB) MCB2146026, MCB1925643NSF | Directorate for Mathematical & Physical Sciences | Division of Mathematical Sciences (DMS) DMS2151678NSF | ENG/OAD | Division of Civil, Mechanical and Manufacturing Innovation (CMMI) CMMI1825941U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM133840
6 · The paper itself

Abstract

Cryogenic electron microscopy (cryo-EM) has now been widely used for determining multichain protein complexes. However, modeling a large complex structure, such as those with more than ten chains, is challenging, particularly when the map resolution decreases. Here we present DiffModeler, a fully automated method for modeling large protein complex structures. DiffModeler employs a diffusion model for backbone tracing and integrates AlphaFold2-predicted single-chain structures for structure fitting. DiffModeler showed an average template modeling score of 0.88 and 0.91 for two datasets of cryo-EM maps of 0-5 Å resolution and 0.92 for intermediate resolution maps (5-10 Å), substantially outperforming existing methodologies. Further benchmarking at low resolutions (10-20 Å) confirms its versatility, demonstrating plausible performance.

Indexed as

Cryoelectron MicroscopyModels, MolecularAlgorithmsDiffusionMacromolecular SubstancesProtein ConformationProteinsSoftwareMacromolecular SubstancesProteins

Identifiers

PMID39433880
PMCPMC12814867

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Registered trials

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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.