Evidence map›Paper›PMID 31160591›Full record

ArticleNature communications2019

Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution.

Xiao Fan, Jia Wang, Xing Zhang, Zi Yang, Jin-Can Zhang, Lingyun Zhao, Hai-Lin Peng, Jianlin Lei, Hong-Wei Wang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
17.9field-weighted citation impact, top 1% 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

83 citing papers in PubMed, 170 citations in OpenAlex.

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  18. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
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  20. Assembly-enhanced recognition: A biomimetic pathway to achieve ultrahigh affinities.Proceedings of the National Academy of Sciences of the United States of America · 2025
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23 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

9 authors at 4 institutions in 2 countries.

Xiao FanMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0001-9855-1641
Jia WangMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Xing ZhangMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Zi YangMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Jin-Can ZhangAcademy for Advanced Interdisciplinary Studies, Peking University, Beijing, 100871, China.
Lingyun ZhaoMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Hai-Lin PengAcademy for Advanced Interdisciplinary Studies, Peking University, Beijing, 100871, China.ORCID http://orcid.org/0000-0003-1569-0238
Jianlin LeiMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China. jllei@tsinghua.edu.cn.ORCID http://orcid.org/0000-0002-9384-8742
Hong-Wei WangMinistry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084, China. hongweiwang@tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-9494-8780
Tsinghua University · CNCenter for Life Sciences · CNKing Center · USPeking University · CN

Funding

Beijing Municipal Science and Technology Commission Z161100000116034Ministry of Science and Technology of the People's Republic of China (Chinese Ministry of Science and Technology) 2016YFA0501100
6 · The paper itself

Abstract

The fast development of single-particle cryogenic electron microscopy (cryo-EM) has made it more feasible to obtain the 3D structure of well-behaved macromolecules with a molecular weight higher than 300 kDa at ~3 Å resolution. However, it remains a challenge to obtain the high-resolution structures of molecules smaller than 200 kDa using single-particle cryo-EM. In this work, we apply the Cs-corrector-VPP-coupled cryo-EM to study the 52 kDa streptavidin (SA) protein supported on a thin layer of graphene and embedded in vitreous ice. We are able to solve both the apo-SA and biotin-bound SA structures at near-atomic resolution using single-particle cryo-EM. We demonstrate that the method has the potential to determine the structures of molecules as small as 39 kDa.

Indexed as

BiotinCryoelectron MicroscopyGraphiteMacromolecular SubstancesModels, MolecularMolecular ConformationSingle Molecule ImagingStreptavidinBiotinGraphiteMacromolecular SubstancesStreptavidin

Identifiers

PMID31160591
PMCPMC6546690
OpenAlexW2901198387

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.