Evidence map›Paper›PMID 33645535›Full record

ReviewActa crystallographica. Section D, Structural biology2021

Macromolecular crystallography using microcrystal electron diffraction.

Max T B Clabbers, Hongyi Xu

Abstract readReview
In one paragraph

Review in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Structure determination of a DNA crystal by MicroED.Structure (London, England : 1993) · 2023
    Article
  9. Review
  10. DIALS as a toolkit.Protein science : a publication of the Protein Society · 2022
    Article
  11. 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

2 authors.

Max T B ClabbersDepartment of Materials and Environmental Chemistry, Stockholm University, 106 91 Stockholm, Sweden.ORCID 0000-0002-5466-6508
Hongyi XuDepartment of Materials and Environmental Chemistry, Stockholm University, 106 91 Stockholm, Sweden.ORCID 0000-0002-8271-3906

Funding

Knut och Alice Wallenbergs Stiftelse 2018.0237Science for Life Laboratory MicroED@SciLifeLabVetenskapsrådet 2017-05333Vetenskapsrådet 2019-00815
6 · The paper itself

Abstract

Microcrystal electron diffraction (MicroED) has recently emerged as a promising method for macromolecular structure determination in structural biology. Since the first protein structure was determined in 2013, the method has been evolving rapidly. Several protein structures have been determined and various studies indicate that MicroED is capable of (i) revealing atomic structures with charges, (ii) solving new protein structures by molecular replacement, (iii) visualizing ligand-binding interactions and (iv) determining membrane-protein structures from microcrystals embedded in lipidic mesophases. However, further development and optimization is required to make MicroED experiments more accurate and more accessible to the structural biology community. Here, we provide an overview of the current status of the field, and highlight the ongoing development, to provide an indication of where the field may be going in the coming years. We anticipate that MicroED will become a robust method for macromolecular structure determination, complementing existing methods in structural biology.

Indexed as

Protein ConformationCrystallizationCrystallographyElectronsMembrane ProteinsModels, MolecularMembrane Proteins3D electron diffractionelectron crystallographymacromolecular crystallographymethods developmentmicrocrystal electron diffraction

Identifiers

PMID33645535
PMCPMC7919406

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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.