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  Forty years in cryoEM of membrane proteins

Kühlbrandt, W. (2022). Forty years in cryoEM of membrane proteins. Microscopy, 71(Supplement 1), i30-i50. doi:10.1093/jmicro/dfab041.

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 Creators:
Kühlbrandt, Werner1, Author                 
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: ATP synthase, electron cryo-microscopy, electron cryo-tomography, membrane structure, photosynthesis, respiratory chain complexes
 Abstract: In a surprisingly short time, electron cryo-microscopy (cryoEM) has developed from a niche technique in structural biology to a mainstream method practiced in a rapidly growing number of laboratories around the world. From its beginnings about 40 years ago, cryoEM has had a major impact on the study of membrane proteins, in particular the energy-converting systems from bacterial, mitochondrial and chloroplast membranes. Early work on two-dimensional crystals attained resolutions ∼3.5 Å, but at present, single-particle cryoEM delivers much more detailed structures without crystals. Electron cryo-tomography of membranes and membrane-associated proteins adds valuable context, usually at lower resolution. The review ends with a brief outlook on future prospects.

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Language(s): eng - English
 Dates: 2021-10-052021-06-072021-11-102022-02-182022-03
 Publication Status: Issued
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1093/jmicro/dfab041
BibTex Citekey: kuhlbrandt_forty_2022
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Title: Microscopy
  Other : Journal of Electron Microscopy
Source Genre: Journal
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Publ. Info: Oxford, UK : Oxford University Press
Pages: - Volume / Issue: 71 (Supplement 1) Sequence Number: - Start / End Page: i30 - i50 Identifier: ISSN: 2050-5698
CoNE: https://pure.mpg.de/cone/journals/resource/2050-5698