Evidence map›Paper›PMID 22197730›Full record

ReviewMethods (San Diego, Calif.)2011

Toward structure determination using membrane-protein nanocrystals and microcrystals.

Mark S Hunter, Petra Fromme

Open access · greenAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Nanocrystalline protein domains via salting-out.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Towards time-resolved serial crystallography in a microfluidic device.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  15. Article
  16. Article
  17. Journal of applied crystallography · 2014
    Article
  18. Transmission electron microscopy as a tool for nanocrystal characterization pre- and post-injector.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Article
  19. Use of transmission electron microscopy to identify nanocrystals of challenging protein targets.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  20. Approaches to automated protein crystal harvesting.Acta crystallographica. Section F, Structural biology communications · 2014
    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

2 authors at 1 institution in 1 country.

Mark S HunterDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA. hunter33@llnl.gov
Petra Fromme
Arizona State University · US

Funding

Project 6 (Holton)U54GM094625 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GIACOMINI, KATHLEEN M · 2010 to 2014
$8.0M
Center for the Rational Design of Membrane Protein CrystallographyU54GM094599 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2014
$6.8M
Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
NIGMS NIH HHS 1R01GM095583-01NIGMS NIH HHS 1U54GM094625-01NIGMS NIH HHS R01 GM095583NIGMS NIH HHS U54 GM094599NIGMS NIH HHS U54 GM094625
6 · The paper itself

Abstract

Membrane proteins are very important for all living cells, being involved in respiration, photosynthesis, cellular uptake and signal transduction, amongst other vital functions. However, less than 300 unique membrane protein structures have been determined to date, often due to difficulties associated with the growth of sufficiently large and well-ordered crystals. This work has been focused on showing the first proof of concept for using membrane protein nanocrystals and microcrystals for high-resolution structure determination. Upon determining that crystals of the membrane protein Photosystem I, which is the largest and most complex membrane protein crystallized to date, exist with only 100 unit cells with sizes of less than 200 nm on an edge, work was done to develop a technique that could exploit the growth of the Photosystem I nanocrystals and microcrystals. Femtosecond X-ray protein nanocrystallography was developed for use at the first high-energy X-ray free electron laser, the LCLS at SLAC National Accelerator Laboratory, in which a liquid jet brought fully-hydrated Photosystem I nanocrystals into the interaction region of the pulsed X-ray source. Diffraction patterns were recorded from millions of individual PSI nanocrystals and data from thousands of different, randomly oriented crystallites were integrated using Monte Carlo integration of the peak intensities. The short pulses (∼70fs) provided by the LCLS allowed the possibility to collect the diffraction data before the onset of radiation damage, exploiting the diffract-before-destroy principle. During the initial experiments at the AMO beamline using 6.9-Å wavelength, Bragg peaks were recorded to 8.5-Å resolution, and an electron-density map was determined that did not show any effects of X-ray-induced radiation damage [94]. Many additional techniques still need to be developed to explore the femtosecond nanocrystallography technique for experimental phasing and time-resolved X-ray crystallography experiments. The first proof-of-principle results for the femtosecond nanocrystallography technique indicate the incredible potential of the technique to offer a new route to the structure determination of membrane proteins.

Indexed as

NanoparticlesAlgorithmsCrystallizationCrystallography, X-RayHumansMembrane ProteinsModels, MolecularPhotosystem I Protein ComplexPowder DiffractionProtein ConformationX-Ray DiffractionMembrane ProteinsPhotosystem I Protein Complex

Identifiers

PMID22197730
PMCPMC3414265
OpenAlexW2089368620

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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.