Evidence map›Paper›PMID 27543495›Full record

ReviewProtein science : a publication of the Protein Society2017

How cryo-electron microscopy and X-ray crystallography complement each other.

Hong-Wei Wang, Jia-Wei Wang

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
–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

79 citing papers in PubMed, 1 synthesis or guideline pooled it.

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  14. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
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19 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.

Hong-Wei WangBeijing Advanced Innovation Center for Structural Biology, Ministry of Education Key Laboratory of Protein Sciences School of Life Sciences, Tsinghua University, Beijing, 100084.ORCID 0000-0001-6529-5629
Jia-Wei WangBeijing Advanced Innovation Center for Structural Biology, Ministry of Education Key Laboratory of Protein Sciences School of Life Sciences, Tsinghua University, Beijing, 100084.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

With the ability to resolve structures of macromolecules at atomic resolution, X-ray crystallography has been the most powerful tool in modern structural biology. At the same time, recent technical improvements have triggered a resolution revolution in the single particle cryo-EM method. While the two methods are different in many respects, from sample preparation to structure determination, they both have the power to solve macromolecular structures at atomic resolution. It is important to understand the unique advantages and caveats of the two methods in solving structures and to appreciate the complementary nature of the two methods in structural biology. In this review we provide some examples, and discuss how X-ray crystallography and cryo-EM can be combined in deciphering structures of macromolecules for our full understanding of their biological mechanisms.

Indexed as

Cryoelectron MicroscopyCrystallography, X-Raycryo-EMprotein structure determinationstructural biologystructure determination methodsX-ray and electron scatteringX-ray crystallography

Identifiers

PMID27543495
PMCPMC5192981

What OpenQuestion holds

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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.