Evidence map›Paper›PMID 39927816›Full record

ReviewBiochemical Society transactions2025

Advancing structure modeling from cryo-EM maps with deep learning.

Shu Li, Genki Terashi, Zicong Zhang, Daisuke Kihara

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Accurate Macromolecular Complex Modeling for Cryo-EM with CryoZeta.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Shu LiDepartment of Computer Science, Purdue University, West Lafayette, IN, U.S.A.ORCID 0000-0003-4667-6164
Genki TerashiDepartment of Biological Sciences, Purdue University, West Lafayette, IN, U.S.A.ORCID 0000-0002-5339-909X
Zicong ZhangDepartment of Computer Science, Purdue University, West Lafayette, IN, U.S.A.ORCID 0000-0002-9545-2944
Daisuke KiharaDepartment of Computer Science, Purdue University, West Lafayette, IN, U.S.A.ORCID 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 GM133840
6 · The paper itself

Abstract

Cryo-electron microscopy (cryo-EM) has revolutionized structural biology by enabling the determination of biomolecular structures that are challenging to resolve using conventional methods. Interpreting a cryo-EM map requires accurate modeling of the structures of underlying biomolecules. Here, we concisely discuss the evolution and current state of automatic structure modeling from cryo-EM density maps. We classify modeling methods into two categories: de novo modeling methods from high-resolution maps (better than 5 Å) and methods that model by fitting individual structures of component proteins to maps at lower resolution (worse than 5 Å). Special attention is given to the role of deep learning in the modeling process, highlighting how AI-driven approaches are transformative in cryo-EM structure modeling. We conclude by discussing future directions in the field.

Indexed as

Cryoelectron MicroscopyDeep LearningModels, MolecularProteinsProtein ConformationProteinsAIartificial intelligencecryo-EMdeep learningstructure modelingstructure validation

Identifiers

PMID39927816
PMCPMC12224893

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.