Evidence map›Paper›PMID 26144225›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Do protein crystals nucleate within dense liquid clusters?

Dominique Maes, Maria A Vorontsova, Marco A C Potenza, Tiziano Sanvito, Mike Sleutel, Marzio Giglio, Peter G Vekilov

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. IntegratedIndustrial & engineering chemistry research · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
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  8. Review
  9. Article
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  11. The pathway from the solution to the steps.Journal of crystal growth · 2022
    Article
  12. Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022
    Review
  13. Crystal nucleation: Rare made common and captured by Raman.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Protein conformation and biomolecular condensates.Current research in structural biology · 2022
    Review
  16. Mesoscopic protein-rich clusters host the nucleation of mutant p53 amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Review
  19. 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

7 authors.

Dominique MaesStructural Biology Brussels (SBB), Vrije Universiteit Brussel, 1050 Brussels, Belgium.
Maria A VorontsovaDepartment of Chemical and Biomolecular Engineering, University of Houston, Houston, TX 77204, USA.
Marco A C PotenzaDipartimento de Fisica, Universita di Milano, 20133 Milano, Italy.
Tiziano SanvitoDipartimento de Fisica, Universita di Milano, 20133 Milano, Italy.
Mike SleutelStructural Biology Brussels (SBB), Vrije Universiteit Brussel, 1050 Brussels, Belgium.
Marzio GiglioDipartimento de Fisica, Universita di Milano, 20133 Milano, Italy.
Peter G VekilovStructural Biology Brussels (SBB), Vrije Universiteit Brussel, 1050 Brussels, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-dense liquid clusters are regions of high protein concentration that have been observed in solutions of several proteins. The typical cluster size varies from several tens to several hundreds of nanometres and their volume fraction remains below 10(-3) of the solution. According to the two-step mechanism of nucleation, the protein-rich clusters serve as locations for and precursors to the nucleation of protein crystals. While the two-step mechanism explained several unusual features of protein crystal nucleation kinetics, a direct observation of its validity for protein crystals has been lacking. Here, two independent observations of crystal nucleation with the proteins lysozyme and glucose isomerase are discussed. Firstly, the evolutions of the protein-rich clusters and nucleating crystals were characterized simultaneously by dynamic light scattering (DLS) and confocal depolarized dynamic light scattering (cDDLS), respectively. It is demonstrated that protein crystals appear following a significant delay after cluster formation. The cDDLS correlation functions follow a Gaussian decay, indicative of nondiffusive motion. A possible explanation is that the crystals are contained inside large clusters and are driven by the elasticity of the cluster surface. Secondly, depolarized oblique illumination dark-field microscopy reveals the evolution from liquid clusters without crystals to newly nucleated crystals contained in the clusters to grown crystals freely diffusing in the solution. Collectively, the observations indicate that the protein-rich clusters in lysozyme and glucose isomerase solutions are locations for crystal nucleation.

Indexed as

AnimalsChickensCrystallizationCrystallography, X-RayDynamic Light ScatteringLiquid CrystalsMuramidaseMuramidasecrystallizationnucleationprotein-rich clusterstwo-step mechanism

Identifiers

PMID26144225
PMCPMC4498701

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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.