Evidence map›Paper›PMID 23633594›Full record

ArticleActa crystallographica. Section D, Biological crystallography2013

Towards protein-crystal centering using second-harmonic generation (SHG) microscopy.

David J Kissick, Christopher M Dettmar, Michael Becker, Anne M Mulichak, Vadim Cherezov, Stephan L Ginell, Kevin P Battaile, Lisa J Keefe, Robert F Fischetti, Garth J Simpson

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Deep learning applications in protein crystallography.Acta crystallographica. Section A, Foundations and advances · 2024
    Review
  3. Low-doseIUCrJ · 2020
    Article
  4. Visualization of protein crystals by high-energy phase-contrast X-ray imaging.Acta crystallographica. Section D, Structural biology · 2019
    Article
  5. Article
  6. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  7. Article
  8. The complex analysis of X-ray mesh scans for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2018
    Article
  9. Article
  10. Article
  11. Intercalating dyes for enhanced contrast in second-harmonic generation imaging of protein crystals.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  12. Identifying, studying and making good use of macromolecular crystals.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  13. Kinetic trapping of metastable amino acid polymorphs.Journal of the American Chemical Society · 2014
    Article
  14. Approaches to automated protein crystal harvesting.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  15. Article
  16. Exploiting Microbeams for Membrane Protein Structure Determination.Advances in experimental medicine and biology
    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

10 authors.

David J KissickDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Christopher M Dettmar
Michael Becker
Anne M Mulichak
Vadim Cherezov
Stephan L Ginell
Kevin P Battaile
Lisa J Keefe
Robert F Fischetti
Garth J Simpson

Funding

JCSG Center:Innovative Membrane Protein Technology (RMI)P50GM073197 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2004 to 2013
$26.8M
Nonlinear Optical Imaging for Guiding Protein Structure DeterminationR01GM103401 · NIGMS · PURDUE UNIVERSITY · PI SIMPSON, GARTH JASON · 2012 to 2018
$1.7M
NIGMS NIH HHS P50 GM073197NIGMS NIH HHS R01 GM103401NIGMS NIH HHS R01GM103401NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The potential of second-harmonic generation (SHG) microscopy for automated crystal centering to guide synchrotron X-ray diffraction of protein crystals was explored. These studies included (i) comparison of microcrystal positions in cryoloops as determined by SHG imaging and by X-ray diffraction rastering and (ii) X-ray structure determinations of selected proteins to investigate the potential for laser-induced damage from SHG imaging. In studies using β2 adrenergic receptor membrane-protein crystals prepared in lipidic mesophase, the crystal locations identified by SHG images obtained in transmission mode were found to correlate well with the crystal locations identified by raster scanning using an X-ray minibeam. SHG imaging was found to provide about 2 µm spatial resolution and shorter image-acquisition times. The general insensitivity of SHG images to optical scatter enabled the reliable identification of microcrystals within opaque cryocooled lipidic mesophases that were not identified by conventional bright-field imaging. The potential impact of extended exposure of protein crystals to five times a typical imaging dose from an ultrafast laser source was also assessed. Measurements of myoglobin and thaumatin crystals resulted in no statistically significant differences between structures obtained from diffraction data acquired from exposed and unexposed regions of single crystals. Practical constraints for integrating SHG imaging into an active beamline for routine automated crystal centering are discussed.

Indexed as

AnimalsCrystallography, X-RayHorsesImage Processing, Computer-AssistedMicroscopyMyoglobinProtein ConformationProteinsReceptors, Adrenergic, beta-2SynchrotronsX-Ray DiffractionMyoglobinProteinsReceptors, Adrenergic, beta-2crystal centeringimagingsecond-harmonic generation microscopy

Identifiers

PMID23633594
PMCPMC3640472

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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.