Evidence map›Paper›PMID 37890869›Full record

ArticleACS nano2023

High-Resolution Electron Diffraction of Hydrated Protein Crystals at Room Temperature.

Sergi Plana-Ruiz, Alejandro Gómez-Pérez, Monika Budayova-Spano, Daniel L Foley, Joaquim Portillo-Serra, Edgar Rauch, Evangelos Grivas, Dominique Housset, Partha Pratim Das, Mitra L Taheri and 2 more

Abstract read
In one paragraph

Article in ACS nano, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Machine learning for the classification of serial electron diffraction patterns: synthetic data.Acta crystallographica. Section A, Foundations and advances · 2025
    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

12 authors.

Sergi Plana-RuizNanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.ORCID 0000-0002-4047-8362
Alejandro Gómez-PérezNanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.
Monika Budayova-SpanoUniversité Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.ORCID 0000-0002-0967-6213
Daniel L FoleyDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland 21218, United States.
Joaquim Portillo-SerraNanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.
Edgar RauchSIMAP, Grenoble INP, Université Grenoble Alpes, CNRS, F-38000 Grenoble, France.
Evangelos GrivasNanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.
Dominique HoussetUniversité Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.
Partha Pratim DasNanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.ORCID 0000-0002-6110-6322
Mitra L TaheriDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland 21218, United States.ORCID 0000-0001-5349-1411
Stavros NicolopoulosNanoMegas SRPL, Rue Emile Claus 49, Brussels 1050, Belgium.
Wai Li LingUniversité Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.ORCID 0000-0002-4264-5750

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural characterization is crucial to understanding protein function. Compared with X-ray diffraction methods, electron crystallography can be performed on nanometer-sized crystals and can provide additional information from the resulting Coulomb potential map. Whereas electron crystallography has successfully resolved three-dimensional structures of vitrified protein crystals, its widespread use as a structural biology tool has been limited. One main reason is the fragility of such crystals. Protein crystals can be easily damaged by mechanical stress, change in temperature, or buffer conditions as well as by electron irradiation. This work demonstrates a methodology to preserve these nanocrystals in their natural environment at room temperature for electron diffraction experiments as an alternative to existing cryogenic techniques. Lysozyme crystals in their crystallization solution are hermetically sealed

Indexed as

ElectronsProteinsCrystallography, X-RayTemperatureX-Ray DiffractionProteinselectron diffractiongraphene liquid cellliquid phase electron microscopylysozymeprotein electron crystallography

Identifiers

PMID37890869
PMCPMC10753879

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Registered trials

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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.