Size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) has become a powerful method to study the solution structures of biomolecular complexes and heterogeneous samples. In this webinar, we introduce a unique laboratory-based SEC-SAXS setup, tailored for the structural analysis of proteins, macromolecular assemblies, and dynamic mixtures. We will present the instrumental configuration, share best practices for data collection and troubleshooting, and guide participants through the data analysis workflow. Published case studies from our lab will illustrate the practical impact of SEC-SAXS in uncovering structural insights from challenging samples. This session is designed for structural biologists, biochemists, and researchers interested in advanced solution-state biophysics.
Laboratory SEC-SAXS provides unique access to structural data from heterogeneous or unstable macromolecular samples, without relying on synchrotron time.
Instrumentation and method optimization (flow rate, column selection, data synchronization) are critical for maximizing resolution and data quality.
SEC-SAXS is particularly powerful for studying transient complexes, mixtures, and flexible systems, where traditional structural methods may fall short.
Published examples demonstrate its impact in characterizing protein-protein interactions, conformational variability, and oligomeric states in biologically relevant conditions using laboratory SEC-SAXS.