Evidence map›Paper›PMID 27436409›Full record

ArticleJournal of structural biology2016

De Novo modeling in cryo-EM density maps with Pathwalking.

Muyuan Chen, Philip R Baldwin, Steven J Ludtke, Matthew L Baker

Abstract read
In one paragraph

Article in Journal of structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Accurate Macromolecular Complex Modeling for Cryo-EM with CryoZeta.bioRxiv : the preprint server for biology · 2026
    Article
  3. CryoAtom improves model building for cryo-EM.Nature structural & molecular biology · 2026
    Article
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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

4 authors.

Muyuan ChenProgram in Structural and Computational Biology and Molecular Biophysics, United States; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States.
Philip R BaldwinDepartment of Psychology, United States; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States.
Steven J LudtkeVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States.
Matthew L BakerVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, United States. Electronic address: mbaker@bcm.edu.

Funding

3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
SUPPORT AND DEVELOPMENT OF EMAN FOR ELECTRON MICROSCOPY IMAGE PROCESSINGR01GM080139 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LUDTKE, STEVEN J · 2006 to 2022
$5.4M
Atomic Resolution Cryo-EM using Model-Based ConstraintsR21GM100229 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BAKER, MATTHEW LOWELL, LUDTKE, STEVEN J · 2013 to 2014
$430k
NIGMS NIH HHS P41 GM103832NIGMS NIH HHS R01 GM079429NIGMS NIH HHS R01 GM080139NIGMS NIH HHS R21 GM100229
6 · The paper itself

Abstract

As electron cryo-microscopy (cryo-EM) can now frequently achieve near atomic resolution, accurate interpretation of these density maps in terms of atomistic detail has become paramount in deciphering macromolecular structure and function. However, there are few software tools for modeling protein structure from cryo-EM density maps in this resolution range. Here, we present an extension of our original Pathwalking protocol, which can automatically trace a protein backbone directly from a near-atomic resolution (3-6Å) density map. The original Pathwalking approach utilized a Traveling Salesman Problem solver for backbone tracing, but manual adjustment was still required during modeling. In the new version, human intervention is minimized and we provide a more robust approach for backbone modeling. This includes iterative secondary structure identification, termini detection and the ability to model multiple subunits without prior segmentation. Overall, the new Pathwalking procedure provides a more complete and robust tool for annotating protein structure function in near-atomic resolution density maps.

Indexed as

SoftwareAlgorithmsCryoelectron MicroscopyModels, MolecularProtein ConformationProteinsProtein Structure, SecondaryProteinsBackbone modelProtein structure

Identifiers

PMID27436409
PMCPMC5118137

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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.