Evidence map›Paper›PMID 23546618›Full record

ArticleCurrent protocols in protein science2013

Overview of electron crystallography of membrane proteins: crystallization and screening strategies using negative stain electron microscopy.

Brent L Nannenga, Matthew G Iadanza, Breanna S Vollmar, Tamir Gonen

Open access · greenAbstract read
In one paragraph

Article in Current protocols in protein science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2025
    Article
  2. Nucleation limited assembly and polarized growth of abioRxiv : the preprint server for biology · 2025
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  3. Hallucinating symmetric protein assemblies.Science (New York, N.Y.) · 2022
    Article
  4. Article
  5. Studying membrane proteins with MicroED.Biochemical Society transactions · 2022
    Article
  6. Article
  7. Protein Assembly by Design.Chemical reviews · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. From electron crystallography of 2D crystals to MicroED of 3D crystals.Current opinion in colloid & interface science · 2018
    Article
  13. Biophysics reports · 2018
    Article
  14. Article
  15. MicroED opens a new era for biological structure determination.Current opinion in structural biology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Protein structure determination by MicroED.Current opinion in structural biology · 2014
    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

4 authors at 2 institutions in 1 country.

Brent L NannengaJanelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia, USA.
Matthew G Iadanza
Breanna S Vollmar
Tamir Gonen
Janelia Research Campus · USHoward Hughes Medical Institute · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Electron cryomicroscopy, or cryoEM, is an emerging technique for studying the three-dimensional structures of proteins and large macromolecular machines. Electron crystallography is a branch of cryoEM in which structures of proteins can be studied at resolutions that rival those achieved by X-ray crystallography. Electron crystallography employs two-dimensional crystals of a membrane protein embedded within a lipid bilayer. The key to a successful electron crystallographic experiment is the crystallization, or reconstitution, of the protein of interest. This unit describes ways in which protein can be expressed, purified, and reconstituted into well-ordered two-dimensional crystals. A protocol is also provided for negative stain electron microscopy as a tool for screening crystallization trials. When large and well-ordered crystals are obtained, the structures of both protein and its surrounding membrane can be determined to atomic resolution.

Indexed as

Cryoelectron MicroscopyCrystallographyMembrane ProteinsMolecular ConformationNegative StainingMembrane Proteins

Identifiers

PMID23546618
PMCPMC3850493
OpenAlexW2156725731

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.