Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR. Issue 32 (7th July 2017)

• Record Type: Journal Article
• Authors: Zinke, Maximilian; Fricke, Pascal; Samson, Camille; Hwang, Songhwan; Wall, Joseph S.; Lange, Sascha; Zinn‐Justin, Sophie; Lange, Adam
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 32(2017)
• Page Start: 9497
• Page End: 9501
• Publication Date: 2017-07-07
• Subjects: bacteriophage -- gp17.1 -- non-uniform sampling -- protein structures -- solid-state NMR; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201706060
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: 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. Abstract : Tube map revealed : Non‐uniform sparse sampling as low as 2 % allowed the introduction of a four‐dimensional assignment strategy for proton‐detected solid‐state NMR. A complex, large bacteriophage tail‐tube assembly was successfully studied by using this new approach.