Evidence map›Paper›PMID 34981757›Full record

ReviewActa crystallographica. Section D, Structural biology2022

Implications of AlphaFold2 for crystallographic phasing by molecular replacement.

Airlie J McCoy, Massimo D Sammito, Randy J Read

Abstract readReview
In one paragraph

Review in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Slice'N'Dice: maximizing the value of predicted models for structural biologists.Acta crystallographica. Section D, Structural biology · 2025
    Article
  12. Review
  13. SFCalculator: connecting deep generative models and crystallography.bioRxiv : the preprint server for biology · 2025
    Article
  14. How the technologies behind self-driving cars, social networks, ChatGPT, and DALL-E2 are changing structural biology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  15. AlphaFold-guided molecular replacement for solving challenging crystal structures.Acta crystallographica. Section D, Structural biology · 2025
    Article
  16. Structural Biology for Target Identification and Validation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  17. Article
  18. Article
  19. Review
  20. AlphaFold two years on: Validation and impact.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

7 more citing papers are in PubMed but not listed here.

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

3 authors.

Airlie J McCoyDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.
Massimo D SammitoDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0002-8346-9247
Randy J ReadDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0001-8273-0047

Funding

Wellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

The AlphaFold2 results in the 14th edition of Critical Assessment of Structure Prediction (CASP14) showed that accurate (low root-mean-square deviation) in silico models of protein structure domains are on the horizon, whether or not the protein is related to known structures through high-coverage sequence similarity. As highly accurate models become available, generated by harnessing the power of correlated mutations and deep learning, one of the aspects of structural biology to be impacted will be methods of phasing in crystallography. Here, the data from CASP14 are used to explore the prospects for changes in phasing methods, and in particular to explore the prospects for molecular-replacement phasing using in silico models.

Indexed as

Computer SimulationAnimalsComputational BiologyCrystallography, X-RayDeep LearningHumansModels, MolecularMolecular StructureProtein ConformationSoftwareAlphaFold2crystallographic phase problemmolecular replacementprotein structure prediction

Identifiers

PMID34981757
PMCPMC8725160

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.