Evidence map›Paper›PMID 29533227›Full record

ArticleActa crystallographica. Section D, Structural biology2018

ARCIMBOLDO on coiled coils.

Iracema Caballero, Massimo Sammito, Claudia Millán, Andrey Lebedev, Nicolas Soler, Isabel Usón

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. ARCIMBOLDO at low resolution: Verification for coiled coils and globular proteins.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Modes and model building in SHELXE.Acta crystallographica. Section D, Structural biology · 2024
    Article
  11. Article
  12. Journal of applied crystallography · 2023
    Article
  13. Predicted models and CCP4.Acta crystallographica. Section D, Structural biology · 2023
    Article
  14. The CCP4 suite: integrative software for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2023
    Article
  15. Article
  16. Fragment-BasedACS bio & med chem Au · 2023
    Article
  17. Article
  18. Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  19. Article
  20. Verification: model-free phasing with enhanced predicted models in ARCIMBOLDO_SHREDDER.Acta crystallographica. Section D, Structural biology · 2022
    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

6 authors.

Iracema CaballeroStructural Biology Unit, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.
Massimo SammitoStructural Biology Unit, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.
Claudia MillánStructural Biology Unit, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.
Andrey LebedevCCP4, STFC Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0FA, England.
Nicolas SolerStructural Biology Unit, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.ORCID 0000-0003-1137-1213
Isabel UsónStructural Biology Unit, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.

Funding

Generalitat de Catalunya 2014SGR-997Ministerio de Economía y Competitividad BES-2015-071397Ministerio de Economía y Competitividad BES-2016-076329Ministerio de Economía y Competitividad BIO2013-49604-EXPMinisterio de Economía y Competitividad BIO2015-64216-PMinisterio de Economía y Competitividad MDM2014-0435
6 · The paper itself

Abstract

ARCIMBOLDO solves the phase problem by combining the location of small model fragments using Phaser with density modification and autotracing using SHELXE. Mainly helical structures constitute favourable cases, which can be solved using polyalanine helical fragments as search models. Nevertheless, the solution of coiled-coil structures is often complicated by their anisotropic diffraction and apparent translational noncrystallographic symmetry. Long, straight helices have internal translational symmetry and their alignment in preferential directions gives rise to systematic overlap of Patterson vectors. This situation has to be differentiated from the translational symmetry relating different monomers. ARCIMBOLDO_LITE has been run on single workstations on a test pool of 150 coiled-coil structures with 15-635 amino acids per asymmetric unit and with diffraction data resolutions of between 0.9 and 3.0 Å. The results have been used to identify and address specific issues when solving this class of structures using ARCIMBOLDO. Features from Phaser v.2.7 onwards are essential to correct anisotropy and produce translation solutions that will pass the packing filters. As the resolution becomes worse than 2.3 Å, the helix direction may be reversed in the placed fragments. Differentiation between true solutions and pseudo-solutions, in which helix fragments were correctly positioned but in a reverse orientation, was found to be problematic at resolutions worse than 2.3 Å. Therefore, after every new fragment-placement round, complete or sparse combinations of helices in alternative directions are generated and evaluated. The final solution is once again probed by helix reversal, refinement and extension. To conclude, density modification and SHELXE autotracing incorporating helical constraints is also exploited to extend the resolution limit in the case of coiled coils and to enhance the identification of correct solutions. This study resulted in a specialized mode within ARCIMBOLDO for the solution of coiled-coil structures, which overrides the resolution limit and can be invoked from the command line (keyword coiled_coil) or ARCIMBOLDO_LITE task interface in CCP4i.

Indexed as

Computer GraphicsComputer SimulationProtein ConformationSoftwareCrystallography, X-RayHumansModels, MolecularProtein DomainsProteinsProteinsARCIMBOLDOcoiled coilsPhaserphasingSHELXE

Identifiers

PMID29533227
PMCPMC5947760

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Registered trials

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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.