Evidence map›Paper›PMID 33520243›Full record

ArticleIUCrJ2021

Exploiting prior knowledge about biological macromolecules in cryo-EM structure determination.

Dari Kimanius, Gustav Zickert, Takanori Nakane, Jonas Adler, Sebastian Lunz, Carola-Bibiane Schönlieb, Ozan Öktem, Sjors H W Scheres

Abstract read
In one paragraph

Article in IUCrJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Efficient high-resolution refinement in cryo-EM with stochastic gradient descent.Acta crystallographica. Section D, Structural biology · 2025
    Article
  3. Article
  4. InstaMap: instant-NGP for cryo-EM density maps.Acta crystallographica. Section D, Structural biology · 2025
    Article
  5. Article
  6. Article
  7. Autocorrelation analysis for cryo-EM with sparsity constraints: Improved sample complexity and projection-based algorithms.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Real space in cryo-EM: the future is local.Acta crystallographica. Section D, Structural biology · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Density modification of cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2020
    Article
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

8 authors.

Dari KimaniusMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Gustav ZickertDepartment of Mathematics, Royal Institute of Technology (KTH), Sweden.
Takanori NakaneMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID https://orcid.org/0000-0003-2697-2767
Jonas AdlerDeepMind, United Kingdom.
Sebastian LunzDepartment of Applied Mathematics and Theoretical Physics, University of Cambridge, Cambridge, United Kingdom.
Carola-Bibiane SchönliebDepartment of Applied Mathematics and Theoretical Physics, University of Cambridge, Cambridge, United Kingdom.
Ozan ÖktemDepartment of Mathematics, Royal Institute of Technology (KTH), Sweden.
Sjors H W ScheresMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.

Funding

Medical Research Council MC_UP_A025_1013
6 · The paper itself

Abstract

Three-dimensional reconstruction of the electron-scattering potential of biological macromolecules from electron cryo-microscopy (cryo-EM) projection images is an ill-posed problem. The most popular cryo-EM software solutions to date rely on a regularization approach that is based on the prior assumption that the scattering potential varies smoothly over three-dimensional space. Although this approach has been hugely successful in recent years, the amount of prior knowledge that it exploits compares unfavorably with the knowledge about biological structures that has been accumulated over decades of research in structural biology. Here, a regularization framework for cryo-EM structure determination is presented that exploits prior knowledge about biological structures through a convolutional neural network that is trained on known macromolecular structures. This neural network is inserted into the iterative cryo-EM structure-determination process through an approach that is inspired by regularization by denoising. It is shown that the new regularization approach yields better reconstructions than the current state of the art for simulated data, and options to extend this work for application to experimental cryo-EM data are discussed.

Indexed as

3D reconstructioncryo-electron microscopyimage processingimagingsingle-particle cryo-EMstructure determination

Identifiers

PMID33520243
PMCPMC7793004

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.