Evidence map›Paper›PMID 24333899›Full record

ArticleJournal of structural biology2014

Combined approaches to flexible fitting and assessment in virus capsids undergoing conformational change.

Arun Prasad Pandurangan, Shabih Shakeel, Sarah Jane Butcher, Maya Topf

Open access · hybridAbstract read
In one paragraph

Article in Journal of structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Automated Modeling and Validation of Protein Complexes in Cryo-EM Maps.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Journal of applied crystallography · 2015
    Article
  16. Article
  17. 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

4 authors at 3 institutions in 2 countries.

Arun Prasad PanduranganInstitute of Structural and Molecular Biology, Department of Biological Sciences/Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, United Kingdom.
Shabih ShakeelInstitute of Biotechnology, P.O. Box 65 (Viikinkaari 1), FIN-00014 University of Helsinki, Helsinki, Finland.
Sarah Jane ButcherInstitute of Biotechnology, P.O. Box 65 (Viikinkaari 1), FIN-00014 University of Helsinki, Helsinki, Finland.
Maya TopfInstitute of Structural and Molecular Biology, Department of Biological Sciences/Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, United Kingdom. Electronic address: m.topf@cryst.bbk.ac.uk.
University of Helsinki · FIBirkbeck, University of London · GBInstitute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K01692X/1Medical Research Council G0600084
6 · The paper itself

Abstract

Fitting of atomic components into electron cryo-microscopy (cryoEM) density maps is routinely used to understand the structure and function of macromolecular machines. Many fitting methods have been developed, but a standard protocol for successful fitting and assessment of fitted models has yet to be agreed upon among the experts in the field. Here, we created and tested a protocol that highlights important issues related to homology modelling, density map segmentation, rigid and flexible fitting, as well as the assessment of fits. As part of it, we use two different flexible fitting methods (Flex-EM and iMODfit) and demonstrate how combining the analysis of multiple fits and model assessment could result in an improved model. The protocol is applied to the case of the mature and empty capsids of Coxsackievirus A7 (CAV7) by flexibly fitting homology models into the corresponding cryoEM density maps at 8.2 and 6.1Å resolution. As a result, and due to the improved homology models (derived from recently solved crystal structures of a close homolog - EV71 capsid - in mature and empty forms), the final models present an improvement over previously published models. In close agreement with the capsid expansion observed in the EV71 structures, the new CAV7 models reveal that the expansion is accompanied by ∼5° counterclockwise rotation of the asymmetric unit, predominantly contributed by the capsid protein VP1. The protocol could be applied not only to viral capsids but also to many other complexes characterised by a combination of atomic structure modelling and cryoEM density fitting.

Indexed as

CapsidCryoelectron MicroscopyEnterovirusModels, MolecularMolecular Dynamics SimulationProtein ConformationSoftwareCoxsackievirus A7Electron cryo-microscopyFlexible fittingModel assessmentPicornaviridae

Identifiers

PMID24333899
PMCPMC3988922
OpenAlexW1984344225

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.