Evidence map›Paper›PMID 35787556›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Serial crystallography with multi-stage merging of thousands of images.

Alexei S Soares, Yusuke Yamada, Jean Jakoncic, Sean McSweeney, Robert M Sweet, John Skinner, James Foadi, Martin R Fuchs, Dieter K Schneider, Wuxian Shi and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

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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

13 authors at 4 institutions in 3 countries.

Alexei S SoaresCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0002-6565-8503
Yusuke YamadaHigh Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, Japan.ORCID 0000-0002-2651-4005
Jean JakoncicCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0002-6315-0933
Sean McSweeneyCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0002-3758-3161
Robert M SweetCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0001-6087-5376
John SkinnerCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0002-0752-5438
James FoadiUniversity of Bath, Bath, United Kingdom.ORCID 0000-0001-7681-1131
Martin R FuchsCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0001-9784-0927
Dieter K SchneiderCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0003-4014-6066
Wuxian ShiCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0003-4771-4601
Babak AndiCenter for BioMolecular Structure, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0002-7666-639X
Lawrence C AndrewsRonin Institute for Independent Scholarship, Kirkland, Washington, USA.ORCID 0000-0002-4451-1641
Herbert J BernsteinRonin Institute for Independent Scholarship, c/o National Synchrotron Light Source II, Building 745, Brookhaven National Laboratory, Upton, New York, USA.ORCID 0000-0002-0517-8532
Brookhaven National Laboratory · USHigh Energy Accelerator Research Organization · JPRonin Institute · USUniversity of Bath · GB

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MARIUZZA, ROY A · 1998 to 2011
$32.2M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
Dectris N/ANCRR NIH HHS P41 RR012408NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P30GM133893NIGMS NIH HHS P41 GM103473NIGMS NIH HHS P41GM103473NIGMS NIH HHS P41 GM111244NIGMS NIH HHS P41GM111244NIGMS NIH HHS P41RR012408U.S. Department of Energy, Office of Science DE-AC02-98CH10886U.S. Department of Energy, Office of Science E-SC0012704U.S. Department of Energy, Office of Science KP1607011
6 · The paper itself

Abstract

KAMO and BLEND provide particularly effective tools to automatically manage the merging of large numbers of data sets from serial crystallography. The requirement for manual intervention in the process can be reduced by extending BLEND to support additional clustering options such as the use of more accurate cell distance metrics and the use of reflection-intensity correlation coefficients to infer `distances' among sets of reflections. This increases the sensitivity to differences in unit-cell parameters and allows clustering to assemble nearly complete data sets on the basis of intensity or amplitude differences. If the data sets are already sufficiently complete to permit it, one applies KAMO once and clusters the data using intensities only. When starting from incomplete data sets, one applies KAMO twice, first using unit-cell parameters. In this step, either the simple cell vector distance of the original BLEND or the more sensitive NCDist is used. This step tends to find clusters of sufficient size such that, when merged, each cluster is sufficiently complete to allow reflection intensities or amplitudes to be compared. One then uses KAMO again using the correlation between reflections with a common hkl to merge clusters in a way that is sensitive to structural differences that may not have perturbed the unit-cell parameters sufficiently to make meaningful clusters. Many groups have developed effective clustering algorithms that use a measurable physical parameter from each diffraction still or wedge to cluster the data into categories which then can be merged, one hopes, to yield the electron density from a single protein form. Since these physical parameters are often largely independent of one another, it should be possible to greatly improve the efficacy of data-clustering software by using a multi-stage partitioning strategy. Here, one possible approach to multi-stage data clustering is demonstrated. The strategy is to use unit-cell clustering until the merged data are sufficiently complete and then to use intensity-based clustering. Using this strategy, it is demonstrated that it is possible to accurately cluster data sets from crystals that have subtle differences.

Indexed as

AlgorithmsSoftwareCluster AnalysisCrystallography, X-RayProteinsProteinsBLENDclusteringKAMOserial crystallography

Identifiers

PMID35787556
PMCPMC9254899
OpenAlexW4283795730

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.