Evidence map›Paper›PMID 24914168›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2014

Time-resolved crystallography and protein design: signalling photoreceptors and optogenetics.

Keith Moffat

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Protein ensembles link genotype to phenotype.PLoS computational biology · 2019
    Review
  5. Time-Resolved Macromolecular Crystallography at Pulsed X-ray Sources.International journal of molecular sciences · 2019
    Review
  6. Article
  7. Review
  8. Blue protein with red fluorescence.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Article
  10. Diffraction Techniques in Structural Biology.Current protocols in nucleic acid chemistry · 2016
    Review
  11. Article
  12. Ligand and interfacial dynamics in a homodimeric hemoglobin.Structural dynamics (Melville, N.Y.) · 2016
    Article
  13. Towards time-resolved serial crystallography in a microfluidic device.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  14. Journal of applied crystallography · 2014
    Article
  15. Article
  16. The birth of a new field.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Article
  17. Molecular Dynamics Simulations of Macromolecular Crystals.Wiley interdisciplinary reviews. Computational molecular science
    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

1 author.

Keith MoffatDepartment of Biochemistry and Molecular Biology, and BioCARS, University of Chicago, 929 East 57th St., Chicago, IL 60637, USA moffat@cars.uchicago.edu.

Funding

TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR01GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1986 to 2012
$4.7M
Structures, Dynamics and Signaling Mechanisms of Modular PhotoreceptorsR01EY024363 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YANG, XIAOJING · 2014 to 2021
$2.9M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR37GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1995 to 2004
$1.9M
BioCARS: A Synchroton Structural Biology ResourceP41GM103543 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2012 to 2012
$1.1M
NEI NIH HHS R01 EY024363NIGMS NIH HHS GM036452NIGMS NIH HHS GM103543NIGMS NIH HHS P41 GM103543NIGMS NIH HHS R01 GM036452NIGMS NIH HHS R24 GM111072NIGMS NIH HHS R37 GM036452
6 · The paper itself

Abstract

Time-resolved X-ray crystallography and solution scattering have been successfully conducted on proteins on time-scales down to around 100 ps, set by the duration of the hard X-ray pulses emitted by synchrotron sources. The advent of hard X-ray free-electron lasers (FELs), which emit extremely intense, very brief, coherent X-ray pulses, opens the exciting possibility of time-resolved experiments with femtosecond time resolution on macromolecular structure, in both single crystals and solution. The X-ray pulses emitted by an FEL differ greatly in many properties from those emitted by a synchrotron, in ways that at first glance make time-resolved measurements of X-ray scattering with the required accuracy extremely challenging. This opens up several questions which I consider in this brief overview. Are there likely to be chemically and biologically interesting structural changes to be revealed on the femtosecond time-scale? How shall time-resolved experiments best be designed and conducted to exploit the properties of FELs and overcome challenges that they pose? To date, fast time-resolved reactions have been initiated by a brief laser pulse, which obviously requires that the system under study be light-sensitive. Although this is true for proteins of the visual system and for signalling photoreceptors, it is not naturally the case for most interesting biological systems. To generate more biological targets for time-resolved study, can this limitation be overcome by optogenetic, chemical or other means?

Indexed as

ElectronsLasersCrystallography, X-RayOptogeneticsProtein EngineeringProteinsSynchrotronsX-Ray DiffractionProteinscrystallographyfree-electron lasersoptogeneticsreaction initiationsolution scatteringtime-resolved X-ray scattering

Identifiers

PMID24914168
PMCPMC4052877

What OpenQuestion holds

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Registered trials

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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.