Evidence map›Paper›PMID 32807957›Full record

ArticleNature methods2020

Improvement of cryo-EM maps by density modification.

Thomas C Terwilliger, Steven J Ludtke, Randy J Read, Paul D Adams, Pavel V Afonine

Abstract read
In one paragraph

Article in Nature methods, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 216 papers.

0numbers the graph read from it
0cells of the map it votes in
216citing 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

216 citing papers in PubMed.

  1. Structural insights into the coupling mechanism of vectorial COProceedings of the National Academy of Sciences of the United States of America · 2026
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  10. Core-sheath coupling controls flagellar curvature and motility inbioRxiv : the preprint server for biology · 2026
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156 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

5 authors.

Thomas C TerwilligerLos Alamos National Laboratory, Los Alamos, NM, USA. tterwilliger@newmexicoconsortium.org.ORCID http://orcid.org/0000-0001-6384-0320
Steven J LudtkeBaylor College of Medicine, Houston, TX, USA.ORCID http://orcid.org/0000-0002-1903-1574
Randy J ReadCambridge Institute for Medical Research, Cambridge, UK.ORCID http://orcid.org/0000-0001-8273-0047
Paul D AdamsMolecular 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.

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
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
SUPPORT AND DEVELOPMENT OF EMAN FOR ELECTRON MICROSCOPY IMAGE PROCESSINGR01GM080139 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LUDTKE, STEVEN J · 2006 to 2022
$5.4M
Integrated Prediction of Protein Struture at 1D, 2D and 3D LevelsR01GM093123 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI CHENG, JIANLIN · 2010 to 2023
$3.8M
Extending MolProbity Diagnosis & Healing Methods to Empower Better CryoEM & Xray Models at 2.5-4A Resolution, plus Versioned, Redeposited "GEMS" for Important Individual StructuresR35GM131883 · NIGMS · DUKE UNIVERSITY · PI RICHARDSON, DAVID CLAUDE · 2019 to 2022
$1.7M
Building protein structure models for intermediate resolution cryo-electron microscopy mapsR01GM133840 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2020 to 2023
$1.6M
Structural Modeling of Multifarious Protein ComplexesR01GM123055 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2017 to 2020
$1.2M
NIGMS NIH HHS P01 GM063210NIGMS NIH HHS R01 GM079429NIGMS NIH HHS R01 GM080139NIGMS NIH HHS R01 GM093123NIGMS NIH HHS R01 GM123055NIGMS NIH HHS R01 GM133840NIGMS NIH HHS R35 GM131883NIGMS NIH HHS T32 GM008284Wellcome Trust 209407/Z/17/ZWellcome Trust 20947/Z/17/Z
6 · The paper itself

Abstract

A density-modification procedure for improving maps from single-particle electron cryogenic microscopy (cryo-EM) is presented. The theoretical basis of the method is identical to that of maximum-likelihood density modification, previously used to improve maps from macromolecular X-ray crystallography. Key differences from applications in crystallography are that the errors in Fourier coefficients are largely in the phases in crystallography but in both phases and amplitudes in cryo-EM, and that half-maps with independent errors are available in cryo-EM. These differences lead to a distinct approach for combination of information from starting maps with information obtained in the density-modification process. The density-modification procedure was applied to a set of 104 datasets and improved map-model correlation and increased the visibility of details in many of the maps. The procedure requires two unmasked half-maps and a sequence file or other source of information on the volume of the macromolecule that has been imaged.

Indexed as

SoftwareApoferritinsCryoelectron MicroscopyImage Processing, Computer-AssistedProtein ConformationApoferritins

Identifiers

PMID32807957
PMCPMC7484085

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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.