Evidence map›Paper›PMID 22505267›Full record

ArticleActa crystallographica. Section D, Biological crystallography2012

To B or not to B: a question of resolution?

Ethan A Merritt

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Cucurbit[7]uril Enhances Distance Measurements of Spin-Labeled Proteins.Journal of the American Chemical Society · 2023
    Article
  4. Review
  5. Article
  6. Toward Real Real-Space Refinement of Atomic Models.International journal of molecular sciences · 2022
    Article
  7. B-factor accuracy in protein crystal structures.Acta crystallographica. Section D, Structural biology · 2022
    Article
  8. Article
  9. Local and global analysis of macromolecular atomic displacement parameters.Acta crystallographica. Section D, Structural biology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structure of a single-chain H2A/H2B dimer.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Analysis and validation of macromolecular B values.Acta crystallographica. Section D, Structural biology · 2019
    Article
  20. A close look onto structural models and primary ligands of metallo-β-lactamases.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2018
    Review
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

1 author.

Ethan A MerrittDepartment of Biochemistry, University of Washington, Seattle, WA 98195-7742, USA. merritt@u.washington.edu

Funding

Software tools for analysis and visulaization of protein structureR01GM080232 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERRITT, ETHAN A · 2007 to 2010
$1.1M
NIGMS NIH HHS R01 GM080232NIGMS NIH HHS R01GM080232
6 · The paper itself

Abstract

In choosing and refining any crystallographic structural model, there is tension between the desire to extract the most detailed information possible and the necessity to describe no more than what is justified by the observed data. A more complex model is not necessarily a better model. Thus, it is important to validate the choice of parameters as well as validating their refined values. One recurring task is to choose the best model for describing the displacement of each atom about its mean position. At atomic resolution one has the option of devoting six model parameters (a 'thermal ellipsoid') to describe the displacement of each atom. At medium resolution one typically devotes at most one model parameter per atom to describe the same thing (a 'B factor'). At very low resolution one cannot justify the use of even one parameter per atom. Furthermore, this aspect of the structure may be described better by an explicit model of bulk displacements, the most common of which is the translation/libration/screw (TLS) formalism, rather than by assigning some number of parameters to each atom individually. One can sidestep this choice between atomic displacement parameters and TLS descriptions by including both treatments in the same model, but this is not always statistically justifiable. The choice of which treatment is best for a particular structure refinement at a particular resolution can be guided by general considerations of the ratio of model parameters to the number of observations and by specific statistics such as the Hamilton R-factor ratio test.

Indexed as

AnisotropyCrystallography, X-RayModels, Molecular

Identifiers

PMID22505267
PMCPMC3322606

What OpenQuestion holds

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Read underepoch 390

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.