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Title: Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR

Obtaining unambiguous resonance assignments remains a major bottleneck in solid-state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three-dimensional (3D) spectra are used. Here, we present a proton-detected 4D solid-state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non-uniform sampling (as low as 2 %). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20 kDa bacteriophage tail-tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data.
Authors:
 [1] ;  [2] ;  [3] ;  [2] ;  [4] ;  [2] ;  [3] ; ORCiD logo [5]
  1. Leibniz-Forschungsinstitut fur Molekulare Pharmakologie (FMP), Berlin (Germany). Department of Molecular Biophysics
  2. Leibniz-Forschungsinstitut fur Molekulare Pharmakologie (FMP), Berlin (Germany). Department of Molecular Biophysics
  3. University of Paris-Sud, University of Paris-Saclay (France). Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS
  4. Brookhaven National Lab. (BNL), Upton, NY (United States)
  5. Leibniz-Forschungsinstitut fur Molekulare Pharmakologie (FMP), Berlin (Germany). Department of Molecular Biophysics; Humboldt Univ. of Berlin (Germany). Institute of Biology
Publication Date:
Report Number(s):
BNL-114099-2017-JA
Journal ID: ISSN 1433-7851
Grant/Contract Number:
SC0012704
Type:
Accepted Manuscript
Journal Name:
Angewandte Chemie (International Edition)
Additional Journal Information:
Journal Name: Angewandte Chemie (International Edition); Journal Volume: 56; Journal Issue: 32; Journal ID: ISSN 1433-7851
Publisher:
Wiley
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; bacteriophage; gp17.1; non-uniform sampling; protein structures; solid-state NMR
OSTI Identifier:
1376150

Zinke, Maximilian, Fricke, Pascal, Samson, Camille, Hwang, Songhwan, Wall, Joseph S., Lange, Sascha, Zinn-Justin, Sophie, and Lange, Adam. Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR. United States: N. p., Web. doi:10.1002/anie.201706060.
Zinke, Maximilian, Fricke, Pascal, Samson, Camille, Hwang, Songhwan, Wall, Joseph S., Lange, Sascha, Zinn-Justin, Sophie, & Lange, Adam. Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR. United States. doi:10.1002/anie.201706060.
Zinke, Maximilian, Fricke, Pascal, Samson, Camille, Hwang, Songhwan, Wall, Joseph S., Lange, Sascha, Zinn-Justin, Sophie, and Lange, Adam. 2017. "Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR". United States. doi:10.1002/anie.201706060. https://www.osti.gov/servlets/purl/1376150.
@article{osti_1376150,
title = {Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR},
author = {Zinke, Maximilian and Fricke, Pascal and Samson, Camille and Hwang, Songhwan and Wall, Joseph S. and Lange, Sascha and Zinn-Justin, Sophie and Lange, Adam},
abstractNote = {Obtaining unambiguous resonance assignments remains a major bottleneck in solid-state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three-dimensional (3D) spectra are used. Here, we present a proton-detected 4D solid-state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non-uniform sampling (as low as 2 %). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20 kDa bacteriophage tail-tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data.},
doi = {10.1002/anie.201706060},
journal = {Angewandte Chemie (International Edition)},
number = 32,
volume = 56,
place = {United States},
year = {2017},
month = {7}
}