Evidence map›Paper›PMID 36322415›Full record

ArticleActa crystallographica. Section D, Structural biology2022

Putting AlphaFold models to work with phenix.process_predicted_model and ISOLDE.

Robert D Oeffner, Tristan I Croll, Claudia Millán, Billy K Poon, Christopher J Schlicksup, Randy J Read, Tom C Terwilliger

Abstract read
In one paragraph

Article 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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Alphafuser: a parsimonious approach to predicting higher-order protein complexes.Acta crystallographica. Section D, Structural biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Slice'N'Dice: maximizing the value of predicted models for structural biologists.Acta crystallographica. Section D, Structural biology · 2025
    Article
  19. Review
  20. 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

7 authors.

Robert D OeffnerDepartment of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Cambridge Biomedical Campus, The Keith Peters Building, Hills Road, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0003-3107-2202
Tristan I CrollDepartment of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Cambridge Biomedical Campus, The Keith Peters Building, Hills Road, Cambridge CB2 0XY, United Kingdom.
Claudia MillánDepartment of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Cambridge Biomedical Campus, The Keith Peters Building, Hills Road, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0002-9283-2220
Billy K PoonMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory (LBNL), Building 33R0349, Berkeley, CA 94720-8235, USA.ORCID 0000-0001-9633-6067
Christopher J SchlicksupMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory (LBNL), Building 33R0349, Berkeley, CA 94720-8235, USA.
Randy J ReadDepartment of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Cambridge Biomedical Campus, The Keith Peters Building, Hills Road, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0001-8273-0047
Tom C TerwilligerNew Mexico Consortium, Los Alamos National Laboratory, 100 Entrada Drive, Los Alamos, NM 87544, USA.ORCID 0000-0001-6384-0320

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
NIGMS NIH HHS P01 GM063210NIH HHS P01GM063210Wellcome Trust 209407/Z/17/ZWellcome Trust Principal Research Fellowship 209407/Z/ 17/Z
6 · The paper itself

Abstract

AlphaFold has recently become an important tool in providing models for experimental structure determination by X-ray crystallography and cryo-EM. Large parts of the predicted models typically approach the accuracy of experimentally determined structures, although there are frequently local errors and errors in the relative orientations of domains. Importantly, residues in the model of a protein predicted by AlphaFold are tagged with a predicted local distance difference test score, informing users about which regions of the structure are predicted with less confidence. AlphaFold also produces a predicted aligned error matrix indicating its confidence in the relative positions of each pair of residues in the predicted model. The phenix.process_predicted_model tool downweights or removes low-confidence residues and can break a model into confidently predicted domains in preparation for molecular replacement or cryo-EM docking. These confidence metrics are further used in ISOLDE to weight torsion and atom-atom distance restraints, allowing the complete AlphaFold model to be interactively rearranged to match the docked fragments and reducing the need for the rebuilding of connecting regions.

Indexed as

SoftwareCryoelectron MicroscopyCrystallography, X-RayModels, MolecularProtein ConformationAlphaFoldconfidence measuresISOLDEPhenixprocess_predicted_model

Identifiers

PMID36322415
PMCPMC9629492

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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.