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  Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy

Khoshouei, M., Danev, R., Plitzko, J. M., & Baumeister, W. (2017). Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy. Journal of Molecular Biology (London), 429(17), 2611-2618. doi:10.1016/j.jmb.2017.07.004.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E759-D Version Permalink: http://hdl.handle.net/21.11116/0000-0001-4FBA-6
Genre: Journal Article

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 Creators:
Khoshouei, Maryam1, Author              
Danev, Radostin1, Author              
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: CRYO-EM STRUCTURE; TRANSMISSION ELECTRON-MICROSCOPY; BEAM-INDUCED MOTION; PHASE-PLATE; 3-DIMENSIONAL MODEL; MOLECULAR SOCIOLOGY; 26S PROTEASOME; RESOLUTION; CRYSTALLOGRAPHY; COMPLEX Biochemistry & Molecular Biology; cryo-electron microscopy; cryo-electron tomography;
 Abstract: Sixty years ago, the first protein structure of myoglobin was determined by John Kendrew and his colleagues; hemoglobin followed shortly thereafter. For quite some time, it seemed that only X-ray crystallography would be capable of determining the structure of proteins to high resolution. In recent years, cryo-electron microscopy has emerged as a viable alternative and indeed in many cases the preferred approach. It is capable of studying proteins that span a size range from several megadaltons to proteins as small as myoglobin and hemoglobin. (C) 2017 Elsevier Ltd. All rights reserved.

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Language(s): eng - English
 Dates: 2017-07-082017
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000408179100005
DOI: 10.1016/j.jmb.2017.07.004
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 429 (17) Sequence Number: - Start / End Page: 2611 - 2618 Identifier: ISSN: 0022-2836
CoNE: /journals/resource/954922646042