ArticleJournal of biomolecular NMR2011
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 53 citations in OpenAlex.
- A random fractionalMagnetic resonance letters · 2026Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR.Chemical science · 2021Review
- Joint X-ray/NMR structure refinement of multidomain/multisubunit systems.Journal of biomolecular NMR · 2019Article
- Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.Journal of visualized experiments : JoVE · 2017Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.Journal of biomolecular NMR · 2016Article
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.Journal of biomolecular NMR · 2015Article
- X-ray crystallography over the past decade for novel drug discovery - where are we heading next?Expert opinion on drug discovery · 2015Review
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Solid state NMR and protein-protein interactions in membranes.Current opinion in structural biology · 2013Review
- Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.Journal of biomolecular NMR · 2013Article
- Solid state NMR strategy for characterizing native membrane protein structures.Accounts of chemical research · 2013Article
- Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer.Journal of molecular biology · 2013Article
- Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures.Protein science : a publication of the Protein Society · 2012Article
- Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals.Nature methods · 2012Article
- Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.Journal of biomolecular NMR · 2012Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
X-ray diffraction and nuclear magnetic resonance spectroscopy (NMR) are the staple methods for revealing atomic structures of proteins. Since crystals of biomolecular assemblies and membrane proteins often diffract weakly and such large systems encroach upon the molecular tumbling limit of solution NMR, new methods are essential to extend structures of such systems to high resolution. Here we present a method that incorporates solid-state NMR restraints alongside of X-ray reflections to the conventional model building and refinement steps of structure calculations. Using the 3.7 Å crystal structure of the integral membrane protein complex DsbB-DsbA as a test case yielded a significantly improved backbone precision of 0.92 Å in the transmembrane region, a 58% enhancement from using X-ray reflections alone. Furthermore, addition of solid-state NMR restraints greatly improved the overall quality of the structure by promoting 22% of DsbB transmembrane residues into the most favored regions of Ramachandran space in comparison to the crystal structure. This method is widely applicable to any protein system where X-ray data are available, and is particularly useful for the study of weakly diffracting crystals.
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