Evidence map›Paper›PMID 28261000›Full record

ArticleCrystal growth & design2016

A Versatile System for High-Throughput In Situ X-ray Screening and Data Collection of Soluble and Membrane-Protein Crystals.

Jana Broecker, Viviane Klingel, Wei-Lin Ou, Aidin R Balo, David J Kissick, Craig M Ogata, Anling Kuo, Oliver P Ernst

Open access · greenAbstract read
In one paragraph

Article in Crystal growth & design, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  5. Low-doseIUCrJ · 2020
    Article
  6. 3D-printed holders forJournal of applied crystallography · 2020
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  7. Article
  8. Article
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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

8 authors at 1 institution in 1 country.

Jana BroeckerDepartment of Biochemistry and Department of Molecular Genetics, University of Toronto , Toronto, Ontario M5S 1A8, Canada.
Viviane KlingelDepartment of Biochemistry and Department of Molecular Genetics, University of Toronto , Toronto, Ontario M5S 1A8, Canada.
Wei-Lin OuDepartment of Biochemistry and Department of Molecular Genetics, University of Toronto , Toronto, Ontario M5S 1A8, Canada.
Aidin R BaloDepartment of Biochemistry and Department of Molecular Genetics, University of Toronto , Toronto, Ontario M5S 1A8, Canada.
David J KissickGM/CA at Advanced Photon Source, Argonne National Laboratory , Lemont, Illinois 60439, United States.
Craig M OgataGM/CA at Advanced Photon Source, Argonne National Laboratory , Lemont, Illinois 60439, United States.
Anling KuoDepartment of Biochemistry and Department of Molecular Genetics, University of Toronto , Toronto, Ontario M5S 1A8, Canada.
Oliver P ErnstDepartment of Biochemistry and Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Biochemistry and Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Argonne National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, in situ data collection has been a major focus of progress in protein crystallography. Here, we introduce the Mylar in situ method using Mylar-based sandwich plates that are inexpensive, easy to make and handle, and show significantly less background scattering than other setups. A variety of cognate holders for patches of Mylar in situ sandwich films corresponding to one or more wells makes the method robust and versatile, allows for storage and shipping of entire wells, and enables automated crystal imaging, screening, and goniometer-based X-ray diffraction data-collection at room temperature and under cryogenic conditions for soluble and membrane-protein crystals grown in or transferred to these plates. We validated the Mylar in situ method using crystals of the water-soluble proteins hen egg-white lysozyme and sperm whale myoglobin as well as the 7-transmembrane protein bacteriorhodopsin from

Identifiers

PMID28261000
PMCPMC5328415
OpenAlexW2528608284

What OpenQuestion holds

Textmetadata
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.