Evidence map›Paper›PMID 21190672›Full record

ArticleBiophysical journal2011

X-ray diffraction from membrane protein nanocrystals.

M S Hunter, D P DePonte, D A Shapiro, R A Kirian, X Wang, D Starodub, S Marchesini, U Weierstall, R B Doak, J C H Spence and 1 more

Abstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Time-Resolved Macromolecular Crystallography at Pulsed X-ray Sources.International journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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
  16. Article
  17. Article
  18. Article
  19. Room temperature femtosecond X-ray diffraction of photosystem II microcrystals.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. Review
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

11 authors.

M S HunterDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona, USA.
D P DePonte
D A Shapiro
R A Kirian
X Wang
D Starodub
S Marchesini
U Weierstall
R B Doak
J C H Spence
P Fromme

Funding

Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
Therapeutic/Mechanistic Role of Ape1 in Germ Cell TumorsR01CA094025 · NCI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI KELLEY, MARK R. · 2003 to 2007
$1.1M
NCI NIH HHS R01 CA094025NIGMS NIH HHS 1R01GM095583-01NIGMS NIH HHS R01 GM095583
6 · The paper itself

Abstract

Membrane proteins constitute > 30% of the proteins in an average cell, and yet the number of currently known structures of unique membrane proteins is < 300. To develop new concepts for membrane protein structure determination, we have explored the serial nanocrystallography method, in which fully hydrated protein nanocrystals are delivered to an x-ray beam within a liquid jet at room temperature. As a model system, we have collected x-ray powder diffraction data from the integral membrane protein Photosystem I, which consists of 36 subunits and 381 cofactors. Data were collected from crystals ranging in size from 100 nm to 2 μm. The results demonstrate that there are membrane protein crystals that contain < 100 unit cells (200 total molecules) and that 3D crystals of membrane proteins, which contain < 200 molecules, may be suitable for structural investigation. Serial nanocrystallography overcomes the problem of x-ray damage, which is currently one of the major limitations for x-ray structure determination of small crystals. By combining serial nanocrystallography with x-ray free-electron laser sources in the future, it may be possible to produce molecular-resolution electron-density maps using membrane protein crystals that contain only a few hundred or thousand unit cells.

Indexed as

X-Ray DiffractionCyanobacteriaNanoparticlesPhotosystem I Protein ComplexPowdersPhotosystem I Protein ComplexPowders

Identifiers

PMID21190672
PMCPMC3010013

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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.