Evidence map›Paper›PMID 36266465›Full record

ArticleNature methods2022

Improved AlphaFold modeling with implicit experimental information.

Thomas C Terwilliger, Billy K Poon, Pavel V Afonine, Christopher J Schlicksup, Tristan I Croll, Claudia Millán, Jane S Richardson, Randy J Read, Paul D Adams

Open access · hybridAbstract read
In one paragraph

Article in Nature methods, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
9.8field-weighted citation impact, top 1% of its field
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

84 citing papers in PubMed, 132 citations in OpenAlex.

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  8. EMProt improves structure determination from cryo-EM maps.Nature structural & molecular biology · 2026
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24 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

9 authors at 4 institutions in 2 countries.

Thomas C TerwilligerNew Mexico Consortium, Los Alamos, NM, USA. tterwilliger@newmexicoconsortium.org.ORCID 0000-0001-6384-0320
Billy K PoonMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Pavel V AfonineMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Christopher J SchlicksupMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Tristan I CrollDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.ORCID 0000-0002-3514-8377
Claudia MillánDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.
Jane S RichardsonDepartment of Biochemistry, Duke University, Durham, NC, USA.ORCID 0000-0002-3311-2944
Randy J ReadDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.ORCID 0000-0001-8273-0047
Paul D AdamsMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID 0000-0001-9333-8219
Lawrence Berkeley National Laboratory · USUniversity of Cambridge · GBDuke University · USLos Alamos National Laboratory · US

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 GM063210Wellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

Machine-learning prediction algorithms such as AlphaFold and RoseTTAFold can create remarkably accurate protein models, but these models usually have some regions that are predicted with low confidence or poor accuracy. We hypothesized that by implicitly including new experimental information such as a density map, a greater portion of a model could be predicted accurately, and that this might synergistically improve parts of the model that were not fully addressed by either machine learning or experiment alone. An iterative procedure was developed in which AlphaFold models are automatically rebuilt on the basis of experimental density maps and the rebuilt models are used as templates in new AlphaFold predictions. We show that including experimental information improves prediction beyond the improvement obtained with simple rebuilding guided by the experimental data. This procedure for AlphaFold modeling with density has been incorporated into an automated procedure for interpretation of crystallographic and electron cryo-microscopy maps.

Indexed as

AlgorithmsProteinsCryoelectron MicroscopyMachine LearningModels, MolecularProtein ConformationProteins

Identifiers

PMID36266465
PMCPMC9636017
OpenAlexW4306888844

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.