ReviewProtein science : a publication of the Protein Society2018
Determination of protein oligomeric structure from small-angle X-ray scattering.
Review in Protein science : a publication of the Protein Society, 2018. 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.
- Bromodomain dimers: A case study of BRD4 and family-wide AlphaFold predictions.Structural dynamics (Melville, N.Y.) · 2026Article
- The many dimeric faces of Lys49 PLAProtein science : a publication of the Protein Society · 2026Article
- Interrogating Encapsulated Protein Structure within Metal-Organic Frameworks at Elevated Temperature.Journal of the American Chemical Society · 2023Article
- Combining small angle X-ray scattering (SAXS) with protein structure predictions to characterize conformations in solution.Methods in enzymology · 2023Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood ClamFrontiers in molecular biosciences · 2022Article
- The DNA binding domain of the Vibrio vulnificus SmcR transcription factor is flexible and binds diverse DNA sequences.Nucleic acids research · 2021Article
- Estimation of the molecular weight of nanoparticles using a single small-angle X-ray scattering measurement on a relative scale.Scientific reports · 2021Article
- Impact of missense mutations in the ALDH7A1 gene on enzyme structure and catalytic function.Biochimie · 2021Review
- Functional and structural characterization of allosteric activation of phospholipase Cε by Rap1A.The Journal of biological chemistry · 2020Article
- Allosteric regulation of lysosomal enzyme recognition by the cation-independent mannose 6-phosphate receptor.Communications biology · 2020Article
- SAXSDom: Modeling multidomain protein structures using small-angle X-ray scattering data.Proteins · 2020Article
- Structural analysis of pathogenic mutations targeting Glu427 of ALDH7A1, the hot spot residue of pyridoxine-dependent epilepsy.Journal of inherited metabolic disease · 2020Article
- Structural analyses of the Group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations.The Journal of biological chemistry · 2020Article
- Changes of Conformation in Albumin with Temperature by Molecular Dynamics Simulations.Entropy (Basel, Switzerland) · 2020Article
- A nucleotide-dependent oligomerization of the Escherichia coli replication initiator DnaA requires residue His136 for remodeling of the chromosomal origin.Nucleic acids research · 2020Article
- Computational reconstruction of atomistic protein structures from coarse-grained models.Computational and structural biotechnology journal · 2020Review
- Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.The Journal of biological chemistry · 2019Article
- Thermodynamic Stability of the Transcription Regulator PaaR2 from Escherichia coli O157:H7.Biophysical journal · 2019Article
- SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale.Protein science : a publication of the Protein Society · 2019Article
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2 authors.
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Abstract
Small-angle X-ray scattering (SAXS) is useful for determining the oligomeric states and quaternary structures of proteins in solution. The average molecular mass in solution can be calculated directly from a single SAXS curve collected on an arbitrary scale from a sample of unknown protein concentration without the need for beamline calibration or protein standards. The quaternary structure in solution can be deduced by comparing the experimental SAXS curve to theoretical curves calculated from proposed models of the oligomer. This approach is especially robust when the crystal structure of the target protein is known, and the candidate oligomer models are derived from the crystal lattice. When SAXS data are obtained at multiple protein concentrations, this analysis can provide insight into dynamic self-association equilibria. Herein, we summarize the computational methods that are used to determine protein molecular mass and quaternary structure from SAXS data. These methods are organized into a workflow and demonstrated with four case studies using experimental SAXS data from the published literature.
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