ArticleProtein science : a publication of the Protein Society2022
EFAMIX, a tool to decompose inline chromatography SAXS data from partially overlapping components.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- New features inJournal of applied crystallography · 2025Article
- Adaptable SEC-SAXS data collection for higher quality structure analysis in solution.Protein science : a publication of the Protein Society · 2024Article
- Development of DNA aptamers for visualization of glial brain tumors and detection of circulating tumor cells.Molecular therapy. Nucleic acids · 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
- Global fitting of multiple data frames from SEC-SAXS to investigate the structure of next-generation nanodiscs.Acta crystallographica. Section D, Structural biology · 2022Article
- 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
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small-angle X-ray scattering (SAXS) is an established technique for structural analysis of biological macromolecules in solution. During the last decade, inline chromatography setups coupling SAXS with size exclusion (SEC-SAXS) or ion exchange (IEC-SAXS) have become popular in the community. These setups allow one to separate individual components in the sample and to record SAXS data from isolated fractions, which is extremely important for subsequent data interpretation, analysis, and structural modeling. However, in case of partially overlapping elution peaks, inline chromatography SAXS may still yield scattering profiles from mixtures of components. The deconvolution of these scattering data into the individual fractions is nontrivial and potentially ambiguous. We describe a cross-platform computer program, EFAMIX, for restoring the scattering and concentration profiles of the components based on the evolving factor analysis (EFA). The efficiency of the program is demonstrated in a number of simulated and experimental SEC-SAXS data sets. Sensitivity and limitations of the method are explored, and its applicability to IEC-SAXS data is discussed. EFAMIX requires minimal user intervention and is available to academic users through the program package ATSAS as from release 3.1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.