Synchrotron SAXS data from solutions of Aldehyde dehydrogenase 7A1 in 50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl, pH 7.8 were collected on the 12.3.1 (SIBYLS) camera on the storage ring Advanced Light Source (ALS) (Berkeley, CA, USA) via the mail-in program. Prior to data collection, an ALDH7A1 sample was passed through a Superdex 200 size exclusion column. Scattering intensities were measured at three nominal protein concentrations using exposure times of 0.5, 1.0, 3.0, and 6.0 s. Scattering curves collected from the protein samples were corrected for background scattering using intensity data collected from the Superdex 200 column effluent. Composite scattering curves for each protein concentration were generated with PRIMUS by scaling and merging the background-corrected high-s region from the 3 s exposure with the low-s region from the 0.5 or 1.0 s exposure.
The FoXS fits have χ values of 1.5 for the tetramer, 12.4 for the dimer, and 1.2 for the 96%/4% tetramer/dimer ensemble.
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