Evidence map›Paper›PMID 26937240›Full record

ArticleJournal of applied crystallography2016

A visible-light-excited fluorescence method for imaging protein crystals without added dyes.

Tiit Lukk, Richard E Gillilan, Doletha M E Szebenyi, Warren R Zipfel

Abstract read
In one paragraph

Article in Journal of applied crystallography, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. A low-cost method for visible fluorescence imaging.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  4. Article
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

4 authors.

Tiit LukkMacCHESS (Macromolecular Diffraction Facility at CHESS), Cornell University , 161 Synchrotron Drive, Ithaca, NY 14853, USA.
Richard E GillilanMacCHESS (Macromolecular Diffraction Facility at CHESS), Cornell University , 161 Synchrotron Drive, Ithaca, NY 14853, USA.
Doletha M E SzebenyiMacCHESS (Macromolecular Diffraction Facility at CHESS), Cornell University , 161 Synchrotron Drive, Ithaca, NY 14853, USA.
Warren R ZipfelDepartment of Biomedical Engineering, Cornell University , B41 Weill Hall, Ithaca, NY 14853, USA.

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Broad wavelength range Zeiss 780 NLO/confocal system for the Cornell Imaging CoreS10OD018516 · OD · CORNELL UNIVERSITY · PI ZIPFEL, WARREN R · 2014 to 2014
$834k
NIGMS NIH HHS P41 GM103485NIH HHS S10 OD018516
6 · The paper itself

Abstract

Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experiments where crystals are cooled to 100 K with a cryostream. In addition to the non-damaging excitation wavelength and low laser power required for imaging, the method can also serve a useful role for differentiating protein crystals from salt crystals in screening trays.

Indexed as

crystal screeningcrystal visualizationfluorescence microscopyprotein crystallography

Identifiers

PMID26937240
PMCPMC4762565

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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.