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FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles
Open accessAbstract
Small Angle X-ray Scattering (SAXS) is an increasingly common and useful technique for structural characterization of molecules in solution. A SAXS experiment determines the scattering intensity of a molecule as a function of spatial frequency, termed SAXS profile. Here, we describe three web servers for modeling atomic structures based on SAXS profiles. FoXS (Fast X-Ray Scattering) rapidly computes a SAXS profile of a given atomistic model and fits it to an experimental profile. FoXSDock docks two rigid protein structures based on a SAXS profile of their complex. MultiFoXS computes a population-weighted ensemble starting from a single input structure by fitting to a SAXS profile of the protein in solution. We describe the interfaces and capabilities of the servers (salilab.org/foxs), followed by demonstrating their application on Interleukin-33 (IL-33) and its primary receptor ST2.
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Accurate assessment of mass, models and resolution by small-angle scattering
Rambo, R. P., & Tainer, J. A. (2013) · Nature · doi:10.1038/nature12070 · Cited by 750
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Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
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Metadata
- Authors
- Schneidman-Duhovny, D., Hammel, M., Tainer, J. A., & Sali, A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-05-05
- Volume
- 44
- Issue
- W1
- Pages
- W424-W429
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2346627216
- Cited by
- 517
- References
- 1
- FWCI
- 20.52
- Type
- journal article
- Language
- en
- Open access
- gold
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