ArticleJournal of biomolecular NMR2008
Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints.
Article in Journal of biomolecular NMR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS.Biophysical journal · 2021Article
- Protein conformational entropy is not slaved to water.Scientific reports · 2020Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Review
- Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains.Nature communications · 2018Article
- 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update.Acta crystallographica. Section D, Structural biology · 2017Article
- Article
- Hybrid Methods in Iron-Sulfur Cluster Biogenesis.Frontiers in molecular biosciences · 2017Review
- Theoretical modeling of multiprotein complexes by iSPOT: Integration of small-angle X-ray scattering, hydroxyl radical footprinting, and computational docking.Journal of structural biology · 2016Article
- Critical assessment of methods of protein structure prediction: Progress and new directions in round XI.Proteins · 2016Article
- Structural Analysis of Multi-Helical RNAs by NMR-SAXS/WAXS: Application to the U4/U6 di-snRNA.Journal of molecular biology · 2016Article
- Protein structure determination by combining sparse NMR data with evolutionary couplings.Nature methods · 2015Article
- Increased resolution of aromatic cross peaks using alternate 13C labeling and TROSY.Journal of biomolecular NMR · 2015Article
- FANTEN: a new web-based interface for the analysis of magnetic anisotropy-induced NMR data.Journal of biomolecular NMR · 2015Article
- The dynamic duo: combining NMR and small angle scattering in structural biology.Protein science : a publication of the Protein Society · 2014Review
- HierarchicalJournal of applied crystallography · 2014Article
- 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
- Conformational heterogeneity in antibody-protein antigen recognition: implications for high affinity protein complex formation.The Journal of biological chemistry · 2014Article
- Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Trends in biochemical sciences · 2013Review
- Sample preparation, data collection, and preliminary data analysis in biomolecular solution X-ray scattering.Current protocols in protein science · 2012Article
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5 authors.
Funding
Abstract
Determination of the accurate three-dimensional structure of large proteins by NMR remains challenging due to a loss in the density of experimental restraints resulting from the often prerequisite perdeuteration. Solution small-angle scattering, which carries long-range translational information, presents an opportunity to enhance the structural accuracy of derived models when used in combination with global orientational NMR restraints such as residual dipolar couplings (RDCs) and residual chemical shift anisotropies (RCSAs). We have quantified the improvements in accuracy that can be obtained using this strategy for the 82 kDa enzyme Malate Synthase G (MSG), currently the largest single chain protein solved by solution NMR. Joint refinement against NMR and scattering data leads to an improvement in structural accuracy as evidenced by a decrease from approximately 4.5 to approximately 3.3 A of the backbone rmsd between the derived model and the high-resolution X-ray structure, PDB code 1D8C. This improvement results primarily from medium-angle scattering data, which encode the overall molecular shape, rather than the lowest angle data that principally determine the radius of gyration and the maximum particle dimension. The effect of the higher angle data, which are dominated by internal density fluctuations, while beneficial, is also found to be relatively small. Our results demonstrate that joint NMR/SAXS refinement can yield significantly improved accuracy in solution structure determination and will be especially well suited for the study of systems with limited NMR restraints such as large proteins, oligonucleotides, or their complexes.
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