Evidence map›Paper›PMID 29754826›Full record

ArticleStructure (London, England : 1993)2018

Atomic Resolution Cryo-EM Structure of β-Galactosidase.

Alberto Bartesaghi, Cecilia Aguerrebere, Veronica Falconieri, Soojay Banerjee, Lesley A Earl, Xing Zhu, Nikolaus Grigorieff, Jacqueline L S Milne, Guillermo Sapiro, Xiongwu Wu and 1 more

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Article
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  4. Review
  5. A NewFoods (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Multi-species cryoEM calibration and workflow verification standard.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  10. Multi-species cryoEM calibration and workflow verification standard.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Factors affecting macromolecule orientations in thin films formed in cryo-EM.Acta crystallographica. Section D, Structural biology · 2024
    Article
  13. Article
  14. Article
  15. Article
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  18. Article
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

11 authors.

Alberto BartesaghiLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Cecilia AguerrebereDepartment of Electrical and Computer Engineering, Duke University, Durham, NC 27708, USA.
Veronica FalconieriLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Soojay BanerjeeLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Lesley A EarlLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Xing ZhuLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Nikolaus GrigorieffJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA.
Jacqueline L S MilneLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Guillermo SapiroDepartment of Electrical and Computer Engineering, Duke University, Durham, NC 27708, USA.
Xiongwu WuLaboratory of Biophysical Chemistry, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892, USA.
Sriram SubramaniamLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA. Electronic address: subramas@mail.nih.gov.

Funding

Technology Development for 3D Electron MicroscopyZIABC010826 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$9.1M
Three-dimensional Structures Of Biological MacromoleculesZIAHL001027 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 2009 to 2025
$8.1M
Imaging cellular assemblies with three-dimensional electron microscopyZIABC010278 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
HIV neutralization and mechanisms of cellular entryZIABC010825 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Structural Analysis of Macromolecular Complexes by Electron MicroscopyZIABC010412 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MILNE, JACQUELINE · 2009 to 2019
$2.7M
Structural Studies of Metabolic Enzymes and Their RegulationZIABC010827 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MILNE, JACQUELINE · 2009 to 2019
$2.7M
Intramural NIH HHS ZIA BC010278Intramural NIH HHS ZIA BC010826NCI NIH HHS ZIA BC010278NCI NIH HHS ZIA BC010825NCI NIH HHS ZIA BC010826NCI NIH HHS ZIA BC010827
6 · The paper itself

Abstract

The advent of direct electron detectors has enabled the routine use of single-particle cryo-electron microscopy (EM) approaches to determine structures of a variety of protein complexes at near-atomic resolution. Here, we report the development of methods to account for local variations in defocus and beam-induced drift, and the implementation of a data-driven dose compensation scheme that significantly improves the extraction of high-resolution information recorded during exposure of the specimen to the electron beam. These advances enable determination of a cryo-EM density map for β-galactosidase bound to the inhibitor phenylethyl β-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at ∼ 1.5 Å resolution. Using this density map in conjunction with constrained molecular dynamics simulations provides a measure of the local flexibility of the non-covalently bound inhibitor and offers further opportunities for structure-guided inhibitor design.

Indexed as

beta-GalactosidaseBinding SitesCryoelectron MicroscopyCrystallography, X-RayDrug DesignModels, MolecularMolecular Dynamics SimulationProtein ConformationThiogalactosidesbeta-GalactosidaseThiogalactosidesatomic resolutioncomputer-aided drug discoverydrift correctiondrug discoveryhigh-resolution protein structureprecision medicineradiation damagesingle-particle cryo-EM

Identifiers

PMID29754826
PMCPMC6129192

What OpenQuestion holds

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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.