Evidence map›Paper›PMID 25286844›Full record

ArticleActa crystallographica. Section D, Biological crystallography2014

Metrics for comparison of crystallographic maps.

Alexandre Urzhumtsev, Pavel V Afonine, Vladimir Y Lunin, Thomas C Terwilliger, Paul D Adams

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Explicit correction of severely non-uniform distributions of cryo-EM views.Acta crystallographica. Section D, Structural biology · 2026
    Article
  4. Article
  5. Structural basis for partial agonism in 5-HTNature structural & molecular biology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Density modification of cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. New tools for the analysis and validation of cryo-EM maps and atomic models.Acta crystallographica. Section D, Structural biology · 2018
    Article
  15. Real-space refinement in PHENIX for cryo-EM and crystallography.Acta crystallographica. Section D, Structural biology · 2018
    Article
  16. Automated map sharpening by maximization of detail and connectivity.Acta crystallographica. Section D, Structural biology · 2018
    Article
  17. Article
  18. Review
  19. Polder maps: improving OMIT maps by excluding bulk solvent.Acta crystallographica. Section D, Structural biology · 2017
    Article
  20. 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

5 authors.

Alexandre UrzhumtsevCentre for Integrative Biology, Department of Integrated Structural Biology, IGMBC, CNRS UMR 7104-INSERM U964-Université de Strasbourg, 1 Rue Laurent Fries, BP 10142, 67404 Illkirch, France.
Pavel V AfonineLawrence Berkeley National Laboratory, One Cyclotron Road, BLDG 64R0121, Berkeley, CA 94720, USA.
Vladimir Y LuninInstitute of Mathematical Problems of Biology, Russian Academy of Sciences, Pushchino 142290, Russian Federation.
Thomas C TerwilligerLos Alamos National Laboratory, Los Alamos, NM 87545-0001, USA.
Paul D AdamsLawrence Berkeley National Laboratory, One Cyclotron Road, BLDG 64R0121, Berkeley, CA 94720, USA.

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
NIGMS NIH HHS P01 GM063210
6 · The paper itself

Abstract

Numerical comparison of crystallographic contour maps is used extensively in structure solution and model refinement, analysis and validation. However, traditional metrics such as the map correlation coefficient (map CC, real-space CC or RSCC) sometimes contradict the results of visual assessment of the corresponding maps. This article explains such apparent contradictions and suggests new metrics and tools to compare crystallographic contour maps. The key to the new methods is rank scaling of the Fourier syntheses. The new metrics are complementary to the usual map CC and can be more helpful in map comparison, in particular when only some of their aspects, such as regions of high density, are of interest.

Indexed as

Models, MolecularCrystallography, X-RayFourier AnalysisPeptidesReproducibility of ResultsPeptidescorrelation coefficientscrystallographic contour mapsFourier synthesesmap comparisonrank scalingsigma scale

Identifiers

PMID25286844
PMCPMC4188004

What OpenQuestion holds

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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.