Evidence map›Paper›PMID 25866657›Full record

ArticleIUCrJ2015

Routine phasing of coiled-coil protein crystal structures with AMPLE.

Jens M H Thomas, Ronan M Keegan, Jaclyn Bibby, Martyn D Winn, Olga Mayans, Daniel J Rigden

Abstract read
In one paragraph

Article in IUCrJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. ARCIMBOLDO at low resolution: Verification for coiled coils and globular proteins.Protein science : a publication of the Protein Society · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Implications of AlphaFold2 for crystallographic phasing by molecular replacement.Acta crystallographica. Section D, Structural biology · 2022
    Review
  7. Article
  8. Phasertng: directed acyclic graphs for crystallographic phasing.Acta crystallographica. Section D, Structural biology · 2021
    Article
  9. Article
  10. Helical ensembles outperform ideal helices in molecular replacement.Acta crystallographica. Section D, Structural biology · 2020
    Article
  11. Article
  12. ALIXE: a phase-combination tool for fragment-based molecular replacement.Acta crystallographica. Section D, Structural biology · 2020
    Article
  13. Article
  14. Article
  15. ARCIMBOLDO on coiled coils.Acta crystallographica. Section D, Structural biology · 2018
    Article
  16. Fragon: rapid high-resolution structure determination from ideal protein fragments.Acta crystallographica. Section D, Structural biology · 2018
    Article
  17. Approaches to ab initio molecular replacement of α-helical transmembrane proteins.Acta crystallographica. Section D, Structural biology · 2017
    Article
  18. Article
  19. 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.

Jens M H ThomasInstitute of Integrative Biology, University of Liverpool , Liverpool L69 7ZB, England.
Ronan M KeeganResearch Complex at Harwell, STFC Rutherford Appleton Laboratory , Didcot OX11 0FA, England.
Jaclyn BibbyInstitute of Integrative Biology, University of Liverpool , Liverpool L69 7ZB, England.
Martyn D WinnScience and Technology Facilities Council, Daresbury Laboratory , Warrington WA4 4AD, England.
Olga MayansInstitute of Integrative Biology, University of Liverpool , Liverpool L69 7ZB, England.
Daniel J RigdenInstitute of Integrative Biology, University of Liverpool , Liverpool L69 7ZB, England.

Funding

Biotechnology and Biological Sciences Research Council BB/H01330X/1Biotechnology and Biological Sciences Research Council BB/H013652/1
6 · The paper itself

Abstract

Coiled-coil protein folds are among the most abundant in nature. These folds consist of long wound α-helices and are architecturally simple, but paradoxically their crystallographic structures are notoriously difficult to solve with molecular-replacement techniques. The program AMPLE can solve crystal structures by molecular replacement using ab initio search models in the absence of an existent homologous protein structure. AMPLE has been benchmarked on a large and diverse test set of coiled-coil crystal structures and has been found to solve 80% of all cases. Successes included structures with chain lengths of up to 253 residues and resolutions down to 2.9 Å, considerably extending the limits on size and resolution that are typically tractable by ab initio methodologies. The structures of two macromolecular complexes, one including DNA, were also successfully solved using their coiled-coil components. It is demonstrated that both the ab initio modelling and the use of ensemble search models contribute to the success of AMPLE by comparison with phasing attempts using single structures or ideal polyalanine helices. These successes suggest that molecular replacement with AMPLE should be the method of choice for the crystallo-graphic elucidation of a coiled-coil structure. Furthermore, AMPLE may be able to exploit the presence of a coiled coil in a complex to provide a convenient route for phasing.

Indexed as

ab initio modellingcoiled-coil proteinsmacromolecular complexesmolecular replacementsearch-model ensembles

Identifiers

PMID25866657
PMCPMC4392414

What OpenQuestion holds

Textmetadata
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.