Details:

Alternative Title:
J Struct Biol
Publisher's site:
http://dx.doi.org/10.1016/j.jsb.2015.09.010
Personal Author:
Dambacher, Corey M. ; Lander, Gabriel C.
Dambacher, Corey M. ; Lander, Gabriel C. Less -
Description:
Electron microscopy is commonly employed to determine the subunit organization of large macromolecular assemblies. However, the field lacks a robust molecular labeling methodology for unambiguous identification of constituent subunits. We present a strategy that exploits the unique properties of an unnatural amino acid in order to enable site-specific attachment of a single, readily identifiable protein label at any solvent-exposed position on the macromolecular surface. Using this method, we show clear labeling of a subunit within the 26S proteasome lid subcomplex that has not been amenable to labeling by traditional approaches.
Subject:
[+]
Amino Acids
Article
Click Chemistry
Electron Microscopy
Escherichia Coli
Imaging, Three-Dimensional
Macromolecular Substances
Microscopy, Electron
Models, Molecular
Molecular Labeling
Proteasome Endopeptidase Complex
Proteins
Staining And Labeling
Unnatural Amino Acids

Source:
J Struct Biol. 192(2):151-158
Pubmed ID:
26409249
Pubmed Central ID:
PMC4633364
Document Type:
Journal Article
Funding:
DP2 EB020402/EB/NIBIB NIH HHS/United States ; DP2 EB020402-01/DP/NCCDPHP CDC HHS/United States
DP2 EB020402/EB/NIBIB NIH HHS/United States ; DP2 EB020402-01/DP/NCCDPHP CDC HHS/United States Less -
Collection(s):
CDC Public Access
Main Document Checksum:
[+]
urn:sha256:2fc9c7dd5494ab726826132da2a6d67332d9830fc12ba81b1e59cc2e5853d31a
File Type:

Supporting Files

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  	nihms728932.nxml	xml
  	nihms728932f1.gif	gif
  	nihms728932f1.jpg	jpeg
  	nihms728932f2.gif	gif
  	nihms728932f2.jpg	jpeg

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