Evidence map›Paper›PMID 24914147›Full record

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

Femtosecond crystallography of membrane proteins in the lipidic cubic phase.

Wei Liu, Daniel Wacker, Chong Wang, Enrique Abola, Vadim Cherezov

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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Serial femtosecond crystallography.Nature reviews. Methods primers · 2022
    Article
  7. Article
  8. Serial Crystallography for Structure-Based Drug Discovery.Trends in pharmacological sciences · 2020
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. 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

5 authors.

Wei LiuMarine Drug Research Institute, Huaihai Institute of Technology, Lianyungang 222005, People's Republic of China Department of Integrated Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Daniel WackerDepartment of Integrated Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Chong WangDepartment of Integrated Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Enrique AbolaDepartment of Integrated Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Vadim CherezovDepartment of Integrated Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA vcherezo@scripps.edu.

Funding

JCSG Center:Innovative Membrane Protein Technology (RMI)P50GM073197 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2004 to 2013
$26.8M
Project 3U54GM094618 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STEVENS, RAYMOND C · 2010 to 2014
$17.1M
NIGMS NIH HHS P50 GM073197NIGMS NIH HHS U54 GM094618
6 · The paper itself

Abstract

Despite recent technological advances in heterologous expression, stabilization and crystallization of membrane proteins (MPs), their structural studies remain difficult and require new transformative approaches. During the past two years, crystallization in lipidic cubic phase (LCP) has started gaining a widespread acceptance, owing to the spectacular success in high-resolution structure determination of G protein-coupled receptors (GPCRs) and to the introduction of commercial instrumentation, tools and protocols. The recent appearance of X-ray free-electron lasers (XFELs) has enabled structure determination from substantially smaller crystals than previously possible with minimal effects of radiation damage, offering new exciting opportunities in structural biology. The unique properties of LCP material have been exploited to develop special protocols and devices that have established a new method of serial femtosecond crystallography of MPs in LCP (LCP-SFX). In this method, microcrystals are generated in LCP and streamed continuously inside the same media across the intersection with a pulsed XFEL beam at a flow rate that can be adjusted to minimize sample consumption. Pioneering studies that yielded the first room temperature GPCR structures, using a few hundred micrograms of purified protein, validate the LCP-SFX approach and make it attractive for structure determination of difficult-to-crystallize MPs and their complexes with interacting partners. Together with the potential of femtosecond data acquisition to interrogate unstable intermediate functional states of MPs, LCP-SFX holds promise to advance our understanding of this biomedically important class of proteins.

Indexed as

ElectronsLasersCrystallography, X-RayLipidsMembrane ProteinsProtein ConformationX-Ray DiffractionLipidsMembrane ProteinsG protein-coupled receptorlipidic cubic phasemembrane proteinsserial femtosecond crystallographyX-ray free-electron laser

Identifiers

PMID24914147
PMCPMC4052856

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.