ArticleJournal of applied crystallography2015
Methods for analysis of size-exclusion chromatography-small-angle X-ray scattering and reconstruction of protein scattering.
Article in Journal of applied crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed.
- Beyond Small Molecules: Orchestrating Cell Fate with Engineered Water-Soluble Membrane Proteins.Biomolecules · 2026Article
- SEC-SAXS/MC Ensemble Structural Studies of the Microtubule Binding Protein Cdt1 Show Monomeric, Folded-Over Conformations.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Adaptable SEC-SAXS data collection for higher quality structure analysis in solution.Protein science : a publication of the Protein Society · 2024Article
- SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations.bioRxiv : the preprint server for biology · 2024Article
- Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif.Nature communications · 2024Article
- A complete allosteric map of a GTPase switch in its native cellular network.Cell systems · 2023Article
- MOLASS: Software for automatic processing of matrix data obtained from small-angle X-ray scattering and UV-visible spectroscopy combined with size-exclusion chromatography.Biophysics and physicobiology · 2023Article
- Visualizing and accessing correlated SAXS data sets with Similarity Maps and Simple Scattering web resources.Methods in enzymology · 2023Article
- Recent Advances in Understanding the Structures of Translesion Synthesis DNA Polymerases.Genes · 2022Review
- EFAMIX, a tool to decompose inline chromatography SAXS data from partially overlapping components.Protein science : a publication of the Protein Society · 2022Article
- Recent advances in structural characterization of biomacromolecules in foodsFrontiers in nutrition · 2022Review
- A CRISPR Screen Reveals Resistance Mechanisms to CD3-Bispecific Antibody Therapy.Cancer immunology research · 2021Article
- Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.Journal of structural biology · 2020Article
- Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes.Structure (London, England : 1993) · 2019Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.The Journal of biological chemistry · 2019Article
- Modeling Conformationally Flexible Proteins With X-ray Scattering and Molecular Simulations.Computational and structural biotechnology journal · 2019Review
- Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument.Journal of applied crystallography · 2018Article
- Methods for Physical Characterization of Phase-Separated Bodies and Membrane-less Organelles.Journal of molecular biology · 2018Review
- Recent advances in the UltraScan SOlution MOdeller (US-SOMO) hydrodynamic and small-angle scattering data analysis and simulation suite.European biophysics journal : EBJ · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
Size-exclusion chromatography in line with small-angle X-ray scattering (SEC-SAXS) has emerged as an important method for investigation of heterogeneous and self-associating systems, but presents specific challenges for data processing including buffer subtraction and analysis of overlapping peaks. This paper presents novel methods based on singular value decomposition (SVD) and Guinier-optimized linear combination (LC) to facilitate analysis of SEC-SAXS data sets and high-quality reconstruction of protein scattering directly from peak regions. It is shown that Guinier-optimized buffer subtraction can reduce common subtraction artifacts and that Guinier-optimized linear combination of significant SVD basis components improves signal-to-noise and allows reconstruction of protein scattering, even in the absence of matching buffer regions. In test cases with conventional SAXS data sets for cytochrome c and SEC-SAXS data sets for the small GTPase Arf6 and the Arf GTPase exchange factors Grp1 and cytohesin-1, SVD-LC consistently provided higher quality reconstruction of protein scattering than either direct or Guinier-optimized buffer subtraction. These methods have been implemented in the context of a Python-extensible Mac OS X application known as
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