Evidence map›Paper›PMID 39058381›Full record

ArticleActa crystallographica. Section D, Structural biology2024

Likelihood-based interactive local docking into cryo-EM maps in ChimeraX.

Randy J Read, Eric F Pettersen, Airlie J McCoy, Tristan I Croll, Thomas C Terwilliger, Billy K Poon, Elaine C Meng, Dorothee Liebschner, Paul D Adams

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

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
Eric F PettersenDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.
Airlie J McCoyDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.
Tristan I CrollAltos Labs, Granta Park, Cambridge, United Kingdom.ORCID 0000-0002-3514-8377
Thomas C TerwilligerNew Mexico Consortium, 100 Entrada Drive, Los Alamos, NM 87544, USA.ORCID 0000-0001-6384-0320
Billy K PoonMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0000-0001-9633-6067
Elaine C MengDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.
Dorothee LiebschnerMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0000-0003-3921-3209
Paul D AdamsMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0000-0001-9333-8219

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
Phenix: providing high quality software to the research community for crystallography and cryo-EMR24GM141254 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS · 2021 to 2026
$9.2M
NIGMS NIH HHS P01 GM063210NIGMS NIH HHS P01GM063210NIGMS NIH HHS R24 GM141254NIGMS NIH HHS R24GM141254U.S. Department of Energy DE-AC02-05CH11231Wellcome TrustWellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

The interpretation of cryo-EM maps often includes the docking of known or predicted structures of the components, which is particularly useful when the map resolution is worse than 4 Å. Although it can be effective to search the entire map to find the best placement of a component, the process can be slow when the maps are large. However, frequently there is a well-founded hypothesis about where particular components are located. In such cases, a local search using a map subvolume will be much faster because the search volume is smaller, and more sensitive because optimizing the search volume for the rotation-search step enhances the signal to noise. A Fourier-space likelihood-based local search approach, based on the previously published em_placement software, has been implemented in the new emplace_local program. Tests confirm that the local search approach enhances the speed and sensitivity of the computations. An interactive graphical interface in the ChimeraX molecular-graphics program provides a convenient way to set up and evaluate docking calculations, particularly in defining the part of the map into which the components should be placed.

Indexed as

Cryoelectron MicroscopyMolecular Docking SimulationSoftwareProtein ConformationChimeraXcryo-EMdockingemplace_locallikelihood

Identifiers

PMID39058381
PMCPMC11301754

What OpenQuestion holds

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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.