ArticleThe Journal of chemical physics2009
Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy.
Article in The Journal of chemical physics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Homonuclear J-couplings and heteronuclear structural constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- Atomic-Resolution Structure of the Protein Encoded by Gene V of fd Bacteriophage in Complex with Viral ssDNA Determined by Magic-Angle Spinning Solid-State NMR.Journal of the American Chemical Society · 2023Article
- Article
- Transferred-Rotational-Echo Double Resonance.The journal of physical chemistry. A · 2021Article
- Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.Journal of biomolecular NMR · 2019Article
- Direct amideJournal of biomolecular NMR · 2018Article
- Proton-Assisted Recoupling (PAR) in Peptides and Proteins.The journal of physical chemistry. B · 2017Article
- Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.Nature structural & molecular biology · 2016Article
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Solid-state NMR structure determination from diagonal-compensated, sparsely nonuniform-sampled 4D proton-proton restraints.Journal of the American Chemical Society · 2014Article
- Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Journal of the American Chemical Society · 2013Article
- Selectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR.Journal of biomolecular NMR · 2013Article
- Zero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance.The Journal of chemical physics · 2012Article
- Compensated second-order recoupling: application to third spin assisted recoupling.Physical chemistry chemical physics : PCCP · 2012Article
- Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
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5 authors.
Funding
Abstract
We show that quantitative internuclear (15)N-(13)C distances can be obtained in sufficient quantity to determine a complete, high-resolution structure of a moderately sized protein by magic-angle spinning solid-state NMR spectroscopy. The three-dimensional ZF-TEDOR pulse sequence is employed in combination with sparse labeling of (13)C sites in the beta1 domain of the immunoglobulin binding protein G (GB1), as obtained by bacterial expression with 1,3-(13)C or 2-(13)C-glycerol as the (13)C source. Quantitative dipolar trajectories are extracted from two-dimensional (15)N-(13)C planes, in which approximately 750 cross peaks are resolved. The experimental data are fit to exact theoretical trajectories for spin clusters (consisting of one (13)C and several (15)N each), yielding quantitative precision as good as 0.1 A for approximately 350 sites, better than 0.3 A for another 150, and approximately 1.0 A for 150 distances in the range of 5-8 A. Along with isotropic chemical shift-based (TALOS) dihedral angle restraints, the distance restraints are incorporated into simulated annealing calculations to yield a highly precise structure (backbone RMSD of 0.25+/-0.09 A), which also demonstrates excellent agreement with the most closely related crystal structure of GB1 (2QMT, bbRMSD 0.79+/-0.03 A). Moreover, side chain heavy atoms are well restrained (0.76+/-0.06 A total heavy atom RMSD). These results demonstrate for the first time that quantitative internuclear distances can be measured throughout an entire solid protein to yield an atomic-resolution structure.
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