Evidence map›Paper›PMID 33368005›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2021

Automated Modeling and Validation of Protein Complexes in Cryo-EM Maps.

Tristan Cragnolini, Aaron Sweeney, Maya Topf

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

Tristan CragnoliniInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, UK.
Aaron SweeneyInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, UK.
Maya TopfInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, UK. m.topf@cryst.bbk.ac.uk.

Funding

Medical Research CouncilWellcome Trust 208398/Z/17/ZWellcome Trust 209250/Z/17/Z
6 · The paper itself

Abstract

The resolving power of cryo-EM experiments has dramatically improved in recent years. However, many cryo-EM maps may still not achieve a resolution that is sufficiently high to allow model building directly from the map. Instead, it is common practice to fit an initial atomic model to the map and refine this model. Depending on the resolution and whether the structure suffers from inherent flexibility or experimental limitations, different methods can be applied, to obtain high-quality, well-fitted atomic model of the macromolecular assembly represented by the map, and to assess its properties. In this review, we describe some of these methods, with the main focus on those that have been developed in our group over the last decade.

Indexed as

AlgorithmsCryoelectron MicroscopyModels, MolecularMultiprotein ComplexesProtein ConformationSingle Molecule ImagingMultiprotein ComplexesAssemblyCryo-EMDensity fittingStructure modelingValidation

Identifiers

PMID33368005

What OpenQuestion holds

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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.