Evidence map›Paper›PMID 26960117›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Efficient merging of data from multiple samples for determination of anomalous substructure.

David L Akey, Thomas C Terwilliger, Janet L Smith

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source.Acta crystallographica. Section D, Structural biology · 2019
    Article
  5. Choosing your (Friedel) mates wisely: grouping data sets to improve anomalous signal.Acta crystallographica. Section D, Structural biology · 2019
    Article
  6. Article
  7. Article
  8. Maximum-likelihood determination of anomalous substructures.Acta crystallographica. Section D, Structural biology · 2018
    Article
  9. Article
  10. Contemporary Use of Anomalous Diffraction in Biomolecular Structure Analysis.Methods in molecular biology (Clifton, N.J.) · 2017
    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

3 authors.

David L AkeyLife Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109-2216, USA.
Thomas C TerwilligerBioscience Division, Los Alamos National Laboratory, Mail Stop M888, Los Alamos, NM 87545, USA.
Janet L SmithLife Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109-2216, 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
Structure-function studies of alpha-and flavivirusesP01AI055672 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 2003 to 2010
$18.4M
NCI NIH HHS Y1-CO-1020NIAID NIH HHS P01 AI055672NIAID NIH HHS P01AI055672NIGMS NIH HHS P01 GM063210NIGMS NIH HHS P01GM063210NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Merging of data from multiple crystals has proven to be useful for determination of the anomalously scattering atomic substructure for crystals with weak anomalous scatterers (e.g. S and P) and/or poor diffraction. Strategies for merging data from many samples, which require assessment of sample isomorphism, rely on metrics of variability in unit-cell parameters, anomalous signal correlation and overall data similarity. Local scaling, anomalous signal optimization and data-set weighting, implemented in phenix.scale_and_merge, provide an efficient protocol for merging data from many samples. The protein NS1 was used in a series of trials with data collected from 28 samples for phasing by single-wavelength anomalous diffraction of the native S atoms. The local-scaling, anomalous-optimization protocol produced merged data sets with higher anomalous signal quality indicators than did standard global-scaling protocols. The local-scaled data were also more successful in substructure determination. Merged data quality was assessed for data sets where the multiplicity was reduced in either of two ways: by excluding data from individual crystals (to reduce errors owing to non-isomorphism) or by excluding the last-recorded segments of data from each crystal (to minimize the effects of radiation damage). The anomalous signal was equivalent at equivalent multiplicity for the two procedures, and structure-determination success correlated with anomalous signal metrics. The quality of the anomalous signal was strongly correlated with data multiplicity over a range of 12-fold to 150-fold multiplicity. For the NS1 data, the local-scaling and anomalous-optimization protocol handled sample non-isomorphism and radiation-induced decay equally well.

Indexed as

Crystallography, X-RayFlavivirusProtein ConformationSulfurViral Nonstructural ProteinsNS1 protein, FlavivirusSulfurViral Nonstructural Proteinsanomalous scatteringdata merginglocal scalingsulfur phasing

Identifiers

PMID26960117
PMCPMC4784661

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LicenceCC BY
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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.