Evidence map›Paper›PMID 29533226›Full record

ArticleActa crystallographica. Section D, Structural biology2018

Ensembles generated from crystal structures of single distant homologues solve challenging molecular-replacement cases in AMPLE.

Daniel J Rigden, Jens M H Thomas, Felix Simkovic, Adam Simpkin, Martyn D Winn, Olga Mayans, Ronan M Keegan

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Modes and model building in SHELXE.Acta crystallographica. Section D, Structural biology · 2024
    Article
  3. Predicted models and CCP4.Acta crystallographica. Section D, Structural biology · 2023
    Article
  4. Article
  5. Article
  6. Implications of AlphaFold2 for crystallographic phasing by molecular replacement.Acta crystallographica. Section D, Structural biology · 2022
    Review
  7. Redeployment of automated MrBUMP search-model identification for map fitting in cryo-EM.Acta crystallographica. Section D, Structural biology · 2021
    Article
  8. Introduction to molecular replacement: a time perspective.Acta crystallographica. Section D, Structural biology · 2021
    Review
  9. Helical ensembles outperform ideal helices in molecular replacement.Acta crystallographica. Section D, Structural biology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Molecular replacement using structure predictions from databases.Acta crystallographica. Section D, Structural biology · 2019
    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

7 authors.

Daniel J RigdenInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.ORCID 0000-0002-7565-8937
Jens M H ThomasInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.ORCID 0000-0003-0277-8505
Felix SimkovicInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.ORCID 0000-0003-3430-6828
Adam SimpkinInstitute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.
Martyn D WinnScience and Technology Facilities Council, Daresbury Laboratory, Warrington WA4 4AD, England.ORCID 0000-0003-0496-6796
Olga MayansFachbereich Biologie, Universität Konstanz, 78457 Konstanz, Germany.
Ronan M KeeganResearch Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot OX11 0FA, England.

Funding

Biotechnology and Biological Sciences Research Council BB/H013652/1Biotechnology and Biological Sciences Research Council BB/L009544/1
6 · The paper itself

Abstract

Molecular replacement (MR) is the predominant route to solution of the phase problem in macromolecular crystallography. Although routine in many cases, it becomes more effortful and often impossible when the available experimental structures typically used as search models are only distantly homologous to the target. Nevertheless, with current powerful MR software, relatively small core structures shared between the target and known structure, of 20-40% of the overall structure for example, can succeed as search models where they can be isolated. Manual sculpting of such small structural cores is rarely attempted and is dependent on the crystallographer's expertise and understanding of the protein family in question. Automated search-model editing has previously been performed on the basis of sequence alignment, in order to eliminate, for example, side chains or loops that are not present in the target, or on the basis of structural features (e.g. solvent accessibility) or crystallographic parameters (e.g. B factors). Here, based on recent work demonstrating a correlation between evolutionary conservation and protein rigidity/packing, novel automated ways to derive edited search models from a given distant homologue over a range of sizes are presented. A variety of structure-based metrics, many readily obtained from online webservers, can be fed to the MR pipeline AMPLE to produce search models that succeed with a set of test cases where expertly manually edited comparators, further processed in diverse ways with MrBUMP, fail. Further significant performance gains result when the structure-based distance geometry method CONCOORD is used to generate ensembles from the distant homologue. To our knowledge, this is the first such approach whereby a single structure is meaningfully transformed into an ensemble for the purposes of MR. Additional cases further demonstrate the advantages of the approach. CONCOORD is freely available and computationally inexpensive, so these novel methods offer readily available new routes to solve difficult MR cases.

Indexed as

Protein ConformationSoftwareComputer SimulationCrystallography, X-RayHumansModels, MolecularProteinsProteinsAMPLECONCOORDdistant homologuesmolecular replacementsearch-model ensembles

Identifiers

PMID29533226
PMCPMC5947759

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.