Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2041-1723

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels ; volume:9 ; number:1 ; day:26 ; month:11 ; year:2018 ; pages:1-10 ; date:12.2018
Nature Communications ; 9, Heft 1 (26.11.2018), 1-10, 12.2018

Classification: Biowissenschaften, Biologie

Creator: Stock, Charlott
Hielkema, L.
Tascón, I.
Wunnicke, D.
Oostergetel, G. T.
Azkargorta, M.
Batista Paulino, Cristina
Hänelt, Inga

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41467-018-07319-2

URN: urn:nbn:de:101:1-2019010323561331701736

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:49 AM CEST

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Associated

Stock, Charlott
Hielkema, L.
Tascón, I.
Wunnicke, D.
Oostergetel, G. T.
Azkargorta, M.
Batista Paulino, Cristina
Hänelt, Inga
SpringerLink (Online service)

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Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate

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zweidimensionales bewegtes Bild

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zweidimensionales bewegtes Bild

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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

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Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1

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CryoEM at IUCRJ: a new era

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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

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Other Objects (12)

Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

Cryo-EM analysis of human small ribosomal subunit biogenesis

Statistical Inference of cryo-EM Maps

Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model

Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate

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Manifold methods for cryo-EM image denoising

Invariants for multireference alignment and cryo-EM

CryoEM at IUCRJ: a new era

New Approaches to Cryo-EM Image Processing

Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

Cryo-EM analysis of human small ribosomal subunit biogenesis

Statistical Inference of cryo-EM Maps

Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model

Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate

Determining subunit-subunit interaction from statistics of cryo-EM images: observation of nearest-neighbor coupling in a circadian clock protein complex

Manifold methods for cryo-EM image denoising

Invariants for multireference alignment and cryo-EM

CryoEM at IUCRJ: a new era

New Approaches to Cryo-EM Image Processing

Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

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Statistical Inference of cryo-EM Maps

Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model

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