2.7 Å cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope.


Journal

PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081

Informations de publication

Date de publication:
2020
Historique:
received: 27 11 2019
accepted: 16 04 2020
entrez: 7 5 2020
pubmed: 7 5 2020
medline: 1 8 2020
Statut: epublish

Résumé

Here we present the structure of mouse H-chain apoferritin at 2.7 Å (FSC = 0.143) solved by single particle cryogenic electron microscopy (cryo-EM) using a 200 kV device, the Thermo Fisher Glacios®. This is a compact, two-lens illumination system with a constant power objective lens, without any energy filters or aberration correctors, often thought of as a "screening cryo-microscope". Coulomb potential maps reveal clear densities for main chain carbonyl oxygens, residue side chains (including alternative conformations) and bound solvent molecules. We used a quasi-crystallographic reciprocal space approach to fit model coordinates to the experimental cryo-EM map. We argue that the advantages offered by (a) the high electronic and mechanical stability of the microscope, (b) the high emission stability and low beam energy spread of the high brightness Field Emission Gun (X-FEG), (c) direct electron detection technology and (d) particle-based Contrast Transfer Function (CTF) refinement have contributed to achieving high resolution. Overall, we show that basic electron optical settings for automated cryo-electron microscopy imaging can be used to determine structures approaching atomic resolution.

Identifiants

pubmed: 32374767
doi: 10.1371/journal.pone.0232540
pii: PONE-D-19-33016
pmc: PMC7202636
doi:

Substances chimiques

Protein Subunits 0
Apoferritins 9013-31-4

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0232540

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Farzad Hamdi (F)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Christian Tüting (C)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Dmitry A Semchonok (DA)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Koen M Visscher (KM)

AIMMS Division of Molecular Toxicology, Faculty of Science, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands.

Fotis L Kyrilis (FL)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Annette Meister (A)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.
Institute of Biochemistry and Biotechnology, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Ioannis Skalidis (I)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Lisa Schmidt (L)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Christoph Parthier (C)

Institute of Biochemistry and Biotechnology, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Milton T Stubbs (MT)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.
Institute of Biochemistry and Biotechnology, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

Panagiotis L Kastritis (PL)

ZIK HALOmem, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.
Institute of Biochemistry and Biotechnology, Charles-Tanford-Proteinzentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.
ZIK HALOmem, Biozentrum, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

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Classifications MeSH