Evidence map›Paper›PMID 26436197›Full record

ArticleNature communications2015

Observing the overall rocking motion of a protein in a crystal.

Peixiang Ma, Yi Xue, Nicolas Coquelle, Jens D Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, Dieter Willbold, Jacques-Philippe Colletier, Nikolai R Skrynnikov and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. gmXtal: Cooking Crystals with GROMACS.The protein journal · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Chemical reviews · 2022
    Review
  12. Article
  13. Model-Free or Not?Frontiers in molecular biosciences · 2021
    Review
  14. Article
  15. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance RChemphyschem : a European journal of chemical physics and physical chemistry · 2019
    Article
  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

11 authors at 5 institutions in 4 countries.

Peixiang MaUniversité Grenoble Alpes, IBS, F-38044 Grenoble, France.
Yi XueDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Nicolas CoquelleUniversité Grenoble Alpes, IBS, F-38044 Grenoble, France.
Jens D HallerUniversité Grenoble Alpes, IBS, F-38044 Grenoble, France.
Tairan YuwenDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Isabel AyalaUniversité Grenoble Alpes, IBS, F-38044 Grenoble, France.
Oleg MikhailovskiiDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Dieter WillboldCEA, Institut de Biologie Structurale, F-38044 Grenoble, France.
Jacques-Philippe ColletierUniversité Grenoble Alpes, IBS, F-38044 Grenoble, France.
Nikolai R SkrynnikovDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Paul SchandaUniversité Grenoble Alpes, IBS, F-38044 Grenoble, France.
Université Grenoble Alpes · FRPurdue University West Lafayette · USCEA Grenoble · FRForschungszentrum Jülich · DESt Petersburg University · RU

Funding

European Research Council 311318
6 · The paper itself

Abstract

The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall 'rocking' motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1-100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments.

Indexed as

CrystallizationMotionPolyethylene GlycolsCrystallography, X-RayMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein ConformationUbiquitinPolyethylene GlycolsUbiquitin

Identifiers

PMID26436197
PMCPMC4600728
OpenAlexW2268687656

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.