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  Using 2D Crystals to Analyze the Structure of Membrane Proteins

Collinson, I., Vonck, J., & Hizlan, D. (2013). Using 2D Crystals to Analyze the Structure of Membrane Proteins. In D. Rapaport, & J. M. Herrmann (Eds.), Methods in Molecular Biology (pp. 47-65). New York: Springer Science+Business Media. doi:10.1007/978-1-62703-487-6_4.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D524-7 Version Permalink: https://hdl.handle.net/21.11116/0000-000C-D299-A
Genre: Book Chapter

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 Creators:
Collinson, Ian1, Author           
Vonck, Janet2, Author                 
Hizlan, Dilem3, Author
Affiliations:
1School of Biochemistry, University of Bristol, Bristol, UK, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Istanbul Sehir University, Istanbul, Turkey, ou_persistent22              

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Free keywords: Electron crystallography; Cryo-electron microscopy; 2D crystals; SecYEG; Membrane dynamics; Conformational changes; Active state; Native structure; Three-dimensional maps
 Abstract: Electron crystallography is a powerful technique for studying the structure and function of membrane proteins, not only in the ground state, but also in active conformations. When combined with high-resolution structures obtained by X-ray crystallography, electron crystallography can provide insights into the mechanism of the protein. In this chapter we discuss obtaining a three-dimensional map of membrane proteins by electron crystallography and how to combine these maps with atomic resolution models in order to study the function of membrane proteins. We argue that this approach is particularly powerful as it combines the high resolution attainable by X-ray crystallography with the visualization of the subject in the near-native environment of the membrane, by electron cryo-microscopy. This point has been illustrated by the analysis of the protein translocation complex SecYEG.

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Language(s): eng - English
 Dates: 2013-08-092013
 Publication Status: Issued
 Pages: 19
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-1-62703-487-6_4
PMID: 23996170
 Degree: -

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Title: Methods in Molecular Biology
  Subtitle : Membrane Biogenesis: Methods and Protocols,
Source Genre: Series
 Creator(s):
Rapaport, Doron1, Editor
Herrmann, Johannes M.2, Editor
Affiliations:
1 Interfaculty Institute of Biochemistry, University of Tuebingen, Tuebingen, Germany, ou_persistent22            
2 Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany, ou_persistent22            
Publ. Info: New York : Springer Science+Business Media
Pages: 404 Volume / Issue: 1033 Sequence Number: Chapter 4 Start / End Page: 47 - 65 Identifier: DOI: 10.1007/978-1-62703-487-6
ISBN: 978-1-62703-486-9