Evidence map›Paper›PMID 29227642›Full record

ArticleBiochemistry2018

X-rays in the Cryo-Electron Microscopy Era: Structural Biology's Dynamic Future.

Susannah C Shoemaker, Nozomi Ando

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 1 pooled it
5.7field-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

62 citing papers in PubMed, 1 synthesis or guideline pooled it, 115 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Transformers in RNA structure prediction: A review.Computational and structural biotechnology journal · 2025
    Review
  19. Article
  20. Modulation of Albumin Esterase Activity by Warfarin and Diazepam.International journal of molecular sciences · 2024
    Article

2 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

2 authors at 1 institution in 1 country.

Susannah C ShoemakerProgram in Applied and Computational Mathematics and ‡Department of Chemistry, Princeton University , Princeton, New Jersey 08544, United States.
Nozomi AndoProgram in Applied and Computational Mathematics and ‡Department of Chemistry, Princeton University , Princeton, New Jersey 08544, United States.ORCID 0000-0001-7062-1644
Princeton University · US

Funding

Protein Allostery and Catalysis Beyond Bragg DiffractionR35GM124847 · NIGMS · PRINCETON UNIVERSITY · PI Nozomi Ando · 2017 to 2026
$4.1M
Structural Characterizations of Transient and Heterogeneous Protein ComplexesR00GM100008 · NIGMS · PRINCETON UNIVERSITY · PI ANDO, NOZOMI · 2014 to 2016
$747k
NIGMS NIH HHS R00 GM100008NIGMS NIH HHS R35 GM124847
6 · The paper itself

Abstract

Over the past several years, single-particle cryo-electron microscopy (cryo-EM) has emerged as a leading method for elucidating macromolecular structures at near-atomic resolution, rivaling even the established technique of X-ray crystallography. Cryo-EM is now able to probe proteins as small as hemoglobin (64 kDa) while avoiding the crystallization bottleneck entirely. The remarkable success of cryo-EM has called into question the continuing relevance of X-ray methods, particularly crystallography. To say that the future of structural biology is either cryo-EM or crystallography, however, would be misguided. Crystallography remains better suited to yield precise atomic coordinates of macromolecules under a few hundred kilodaltons in size, while the ability to probe larger, potentially more disordered assemblies is a distinct advantage of cryo-EM. Likewise, crystallography is better equipped to provide high-resolution dynamic information as a function of time, temperature, pressure, and other perturbations, whereas cryo-EM offers increasing insight into conformational and energy landscapes, particularly as algorithms to deconvolute conformational heterogeneity become more advanced. Ultimately, the future of both techniques depends on how their individual strengths are utilized to tackle questions at the frontiers of structural biology. Structure determination is just one piece of a much larger puzzle: a central challenge of modern structural biology is to relate structural information to biological function. In this perspective, we share insight from several leaders in the field and examine the unique and complementary ways in which X-ray methods and cryo-EM can shape the future of structural biology.

Indexed as

AlgorithmsCryoelectron MicroscopyCrystallography, X-RayMacromolecular SubstancesProtein ConformationMacromolecular Substances

Identifiers

PMID29227642
PMCPMC5999524
OpenAlexW2774559011

What OpenQuestion holds

Textmetadata
LicenceTDM
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.