Evidence map›Paper›PMID 28880248›Full record

ArticleInternational journal of molecular sciences2017

X-ray Free Electron Laser Determination of Crystal Structures of Dark and Light States of a Reversibly Photoswitching Fluorescent Protein at Room Temperature.

Christopher D M Hutchison, Violeta Cordon-Preciado, Rhodri M L Morgan, Takanori Nakane, Josie Ferreira, Gabriel Dorlhiac, Alvaro Sanchez-Gonzalez, Allan S Johnson, Ann Fitzpatrick, Clyde Fare and 10 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Serial femtosecond crystallography.Nature reviews. Methods primers · 2022
    Article
  4. Article
  5. Article
  6. Optical control, selection and analysis of population dynamics in ultrafast protein X-ray crystallography.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019
    Article
  7. Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019
    Review
  8. 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

20 authors at 7 institutions in 3 countries.

Christopher D M HutchisonMolecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. christopher.hutchison05@imperial.ac.uk.
Violeta Cordon-PreciadoMolecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. violeta.cordon-preciado@imperial.ac.uk.
Rhodri M L MorganProtein Crystallography Facility, Centre for Structural Biology, Flowers Building, Department of Life Sciences, Imperial College London, London SW7 2AZ, UK. j.ferreira14@imperial.ac.uk.ORCID 0000-0002-4411-6131
Takanori NakaneDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. takanori.nakane@bs.s.u-tokyo.ac.jp.ORCID 0000-0003-2697-2767
Josie FerreiraMolecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. gabriel.dorlhiac13@imperial.ac.uk.
Gabriel DorlhiacMolecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. c.fare12@imperial.ac.uk.
Alvaro Sanchez-GonzalezQuantum Optics and Laser Science Group, Blackett Laboratory, Imperial College, London SW7 2AZ, UK. a.sanchez-gonzalez13@imperial.ac.uk.
Allan S JohnsonQuantum Optics and Laser Science Group, Blackett Laboratory, Imperial College, London SW7 2AZ, UK. allan.s.johnson@gmail.com.ORCID 0000-0002-0711-708X
Ann FitzpatrickDiamond Light Source Ltd., Diamond House, Harwell Science & Innovation Campus, Didcot OX11 0DE, UK. ann.fitzpatrick@diamond.ac.uk.
Clyde FareMolecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
Jon P MarangosQuantum Optics and Laser Science Group, Blackett Laboratory, Imperial College, London SW7 2AZ, UK. j.marangos@imperial.ac.uk.
Chun Hong YoonLCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd., Menlo Park, CA 94025, USA. yoon82@stanford.edu.ORCID 0000-0003-1482-1662
Mark S HunterLCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd., Menlo Park, CA 94025, USA. mhunter2@slac.stanford.edu.
Daniel P DePonteLCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd., Menlo Park, CA 94025, USA. deponte@slac.stanford.edu.
Sébastien BoutetLCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd., Menlo Park, CA 94025, USA. sboutet@slac.stanford.edu.
Shigeki OwadaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Hyogo 679-5148, Japan. osigeki@spring8.or.jp.
Rie TanakaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Hyogo 679-5148, Japan. rie.tanaka.hw@riken.jp.
Kensuke TonoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Hyogo 679-5148, Japan. tono@spring8.or.jp.
So IwataRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Hyogo 679-5148, Japan. s.iwata@spring8.or.jp.
Jasper J van ThorMolecular Biophysics, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. j.vanthor@imperial.ac.uk.
Imperial College London · GBSLAC National Accelerator Laboratory · USSPring-8 · JPDiamond Light Source · GBInstitute of Structural and Molecular Biology · GBKyoto University · JPThe University of Tokyo · JP

Funding

European Research Council 290467
6 · The paper itself

Abstract

The photochromic fluorescent protein Skylan-NS (Nonlinear Structured illumination variant mEos3.1H62L) is a reversibly photoswitchable fluorescent protein which has an unilluminated/ground state with an anionic and cis chromophore conformation and high fluorescence quantum yield. Photo-conversion with illumination at 515 nm generates a meta-stable intermediate with neutral trans-chromophore structure that has a 4 h lifetime. We present X-ray crystal structures of the cis (on) state at 1.9 Angstrom resolution and the trans (off) state at a limiting resolution of 1.55 Angstrom from serial femtosecond crystallography experiments conducted at SPring-8 Angstrom Compact Free Electron Laser (SACLA) at 7.0 keV and 10.5 keV, and at Linac Coherent Light Source (LCLS) at 9.5 keV. We present a comparison of the data reduction and structure determination statistics for the two facilities which differ in flux, beam characteristics and detector technologies. Furthermore, a comparison of droplet on demand, grease injection and Gas Dynamic Virtual Nozzle (GDVN) injection shows no significant differences in limiting resolution. The photoconversion of the on- to the off-state includes both internal and surface exposed protein structural changes, occurring in regions that lack crystal contacts in the orthorhombic crystal form.

Indexed as

LasersCrystallography, X-RayLuminescent ProteinsProtein ConformationTemperatureLuminescent ProteinsLCLSrsFPSACLASFXSkylan-NSXFEL

Identifiers

PMID28880248
PMCPMC5618567
OpenAlexW2751167646

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.