Comparing SAXS modelling approaches on structural transitions in calmodulin protein measured at high-throughput LIX beamline

Abstract

Small-angle X-ray scattering is an increasingly popular technique used to detect protein structures and ensembles in solution. However, the refinement of structures and ensembles against SAXS data is often ambiguous due to the low information content of SAXS data, unknown systematic errors, and unknown scattering contributions from the solvent. At LIX beamline we can perform high throughput measurements reliably and collect data at wider angle (∼3 Å−1) thus accessing the water peak. We use water peak as an internal reference to perform sample to buffer subtraction.