Evidence map›Paper›PMID 30220541›Full record

ArticleStructure (London, England : 1993)2018

Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity.

Dan Ye, Thinh P Le, Brooke Kuei, Chenhui Zhu, Peter H Zwart, Cheng Wang, Enrique D Gomez, Esther W Gomez

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

8 authors.

Dan YeDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Thinh P LeDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Brooke KueiDepartment of Materials Science and Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
Chenhui ZhuAdvanced Light Source, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Peter H ZwartBerkeley Center for Structural Biology, Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA; The Center for Advanced Mathematics for Energy Research Applications, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Cheng WangAdvanced Light Source, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA. Electronic address: cwang2@lbl.gov.
Enrique D GomezDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA; Department of Materials Science and Engineering, The Pennsylvania State University, University Park, PA 16802, USA; Materials Research Institute, The Pennsylvania State University, University Park, PA 16802, USA. Electronic address: edg12@psu.edu.
Esther W GomezDepartment of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA; Department of Biomedical Engineering, The Pennsylvania State University, University Park, PA 16802, USA. Electronic address: ewg10@psu.edu.

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
The Development of Computational Methods for Fluctuation Xray ScatteringR01GM109019 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ZWART, PETRUS H · 2014 to 2018
$1.9M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM109019
6 · The paper itself

Abstract

We introduce resonant soft X-ray scattering (RSoXS) as an approach to study the structure of proteins and other biological molecules in solution. Scattering contrast calculations suggest that RSoXS has comparable or even higher sensitivity than hard X-ray scattering because of contrast generated at the absorption edges of constituent elements, such as carbon and oxygen. Here, we demonstrate that working near the carbon edge reveals the envelope function of bovine serum albumin, using scattering volumes of 10

Indexed as

AnimalsCattleModels, MolecularProtein ConformationSerum Albumin, BovineX-Ray DiffractionSerum Albumin, Bovineenvelope functionNEXAFSprotein structureRSoXSSAXSsmall-angle scatteringsoft X-rays

Identifiers

PMID30220541
PMCPMC8224816

What OpenQuestion holds

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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.