Evidence map›Paper›PMID 24922271›Full record

ArticleNature protocols2014

Porous nucleating agents for protein crystallization.

Sahir Khurshid, Emmanuel Saridakis, Lata Govada, Naomi E Chayen

Abstract read
PubMed Publisher
In one paragraph

Article in Nature protocols, 2014. 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
5.8field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
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  4. Article
  5. Heterogeneous Nucleation in Protein Crystallization.Biomimetics (Basel, Switzerland) · 2023
    Review
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  7. Article
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  13. Review
  14. Review
  15. Protein crystal nucleation in pores.Scientific reports · 2017
    Article
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  17. Article
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  19. Article
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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

4 authors at 2 institutions in 2 countries.

Sahir KhurshidComputational and Systems Medicine, Department of Surgery and Cancer, Faculty of Medicine, Imperial College London, London, UK.
Emmanuel SaridakisLaboratory of Structural and Supramolecular Chemistry, Department of Physical Chemistry, National Centre for Scientific Research 'Demokritos', Athens, Greece.
Lata GovadaComputational and Systems Medicine, Department of Surgery and Cancer, Faculty of Medicine, Imperial College London, London, UK.
Naomi E ChayenComputational and Systems Medicine, Department of Surgery and Cancer, Faculty of Medicine, Imperial College London, London, UK.
Imperial College London · GBNational Centre of Scientific Research "Demokritos" · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solving the structure of proteins is pivotal to achieving success in rational drug design and in other biotechnological endeavors. The most powerful method for determining the structure of proteins is X-ray crystallography, which relies on the availability of high-quality crystals. However, obtaining such crystals is a major hurdle. Nucleation is the crucial prerequisite step, which requires overcoming an energy barrier. The presence in a protein solution of a nucleant, a solid or a semiliquid substance that facilitates overcoming that barrier allows crystals to grow under ideal conditions, paving the way for the formation of high-quality crystals. The use of nucleants provides a unique means for optimizing the diffraction quality of crystals, as well as for discovering new crystallization conditions. We present a protocol for controlling the nucleation of protein crystals that is applicable to a wide variety of nucleation-inducing substances. Setting up crystallization trials using these nucleating agents takes an additional few seconds compared with conventional setup, and it can accelerate crystallization, which typically takes several days to months.

Indexed as

CeramicsCrystallizationFiltrationPhase TransitionPorosityProteinsProtein StabilityX-Ray DiffractionBioglassProteins

Identifiers

PMID24922271
OpenAlexW2081786891

What OpenQuestion holds

Textmetadata
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.