Evidence map›Paper›PMID 24189238›Full record

ReviewActa crystallographica. Section D, Biological crystallography2013

From lows to highs: using low-resolution models to phase X-ray data.

David I Stuart, Nicola G A Abrescia

Open access · hybridAbstract readReview
In one paragraph

Review in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.9field-weighted citation impact, top 6% of its field
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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Integrative Approaches to Study Virus Structures.Sub-cellular biochemistry · 2024
    Review
  2. Article
  3. Article
  4. How cryo-electron microscopy and X-ray crystallography complement each other.Protein science : a publication of the Protein Society · 2017
    Review
  5. Article
  6. Article
  7. Molecular replacement then and now.Acta crystallographica. Section D, Biological crystallography · 2013
    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

2 authors at 2 institutions in 2 countries.

David I StuartDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, England.
Nicola G A Abrescia
CIC bioGUNE · ESUniversity of Oxford · GB

Funding

Medical Research Council G1000099Medical Research Council G1100525Medical Research Council G19/3Wellcome Trust 090532
6 · The paper itself

Abstract

The study of virus structures has contributed to methodological advances in structural biology that are generally applicable (molecular replacement and noncrystallographic symmetry are just two of the best known examples). Moreover, structural virology has been instrumental in forging the more general concept of exploiting phase information derived from multiple structural techniques. This hybridization of structural methods, primarily electron microscopy (EM) and X-ray crystallography, but also small-angle X-ray scattering (SAXS) and nuclear magnetic resonance (NMR) spectroscopy, is central to integrative structural biology. Here, the interplay of X-ray crystallography and EM is illustrated through the example of the structural determination of the marine lipid-containing bacteriophage PM2. Molecular replacement starting from an ~13 Å cryo-EM reconstruction, followed by cycling density averaging, phase extension and solvent flattening, gave the X-ray structure of the intact virus at 7 Å resolution This in turn served as a bridge to phase, to 2.5 Å resolution, data from twinned crystals of the major coat protein (P2), ultimately yielding a quasi-atomic model of the particle, which provided significant insights into virus evolution and viral membrane biogenesis.

Indexed as

Amino Acid SubstitutionModels, MolecularScattering, Small AngleBromusCapsid ProteinsCorticoviridaeCryoelectron MicroscopyCrystallizationCrystallography, X-RayMagnetic Resonance SpectroscopyTobacco Mosaic VirusTobacco necrosis satellite virusTombusvirusCapsid Proteinsdata collectionnoncrystallographic symmetryphasing methodsvirus structure

Identifiers

PMID24189238
PMCPMC3817700
OpenAlexW2162974742

What OpenQuestion holds

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LicenceCC BY
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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.