Low- <i>Q</i> Asymptotic Behavior of the Effective Structure Factor Yields Model-Independent Radius of Interparticle Interaction ( <i>R</i> <sub> <i>i</i> </sub> )
Guinier analysis has been extensively used in academic and industrial research settings to obtain the model-independent size of a polymer, protein, or colloid in solution from small-angle scattering data. Using the Guinier model, the radius of gyration (<i>R</i> <sub><i>g</i></sub> ) is extracted from the form factor at low <i>Q</i>. Here, we develop an analogous approach for analyzing the effective structure factor data at low <i>Q</i> to extract a model-independent radius of interaction potential, <i>R</i> <sub><i>i</i></sub> . Whereas <i>R</i> <sub><i>g</i></sub> describes how spread out the scattering length density distribution of particles is from their center of mass, <i>R</i> <sub><i>i</i></sub> is an effective root-mean-square distance that quantifies how far the interparticle correlation deviates from its ideal gas configuration due to interactions. We demonstrate this novel analysis method by applying it to experimental small-angle neutron scattering data on lysozyme protein solutions. We discuss its broad implications for analysis of low-<i>Q</i> asymptotic X-ray and neutron scattering data, where Guinier analysis is traditionally applied.
Authors
- Wellington Leite (ORCID: https://orcid.org/0000-0002-5674-3968)
- Chelsea E. R. Edwards (ORCID: https://orcid.org/0000-0003-1540-7594)
- Yun Liu (ORCID: https://orcid.org/0000-0002-0944-3153)
Institutions
- Oak Ridge National Laboratory (US)
- National Institute of Standards and Technology (US)
- National Institute of Standards (EG)
- NIST Center for Neutron Research (US)
- University of Delaware (US)
Publication Details
- Journal
- ACS Measurement Science Au
- Published
- 2025-11-07
- DOI
- https://doi.org/10.1021/acsmeasuresciau.5c00099
- Primary Topic
- Enzyme Structure and Function
- Type
- article
- Field-Weighted Citation Impact
- 0.00