Binding structures of SERF1a with the N-terminal fragment of huntingtin exon 1 and NT17-polyQ peptides are revealed using an integrated analysis of size-exclusion-column-based small- and wide-angle X-ray scattering (SEC-SWAXS), NMR, and molecular simulation.

Microgravity was used in an attempt to define the crystal structure of the polyQ repeat of huntingtin alone or bound to MW1, an anti-polyQ Fab. While huntingtin was not crystallized in the experiments, analysis of microgravity-grown and Earth-grown MW1 Fab crystals showed that, on average, microgravity-grown crystals of MW1 Fab showed an increase in size and an improvement in resolution and mosaicity when compared with Earth-grown crystals in one space group, in agreement with data published for other proteins, although the highest overall resolution X-ray data in our experiments were obtained from a crystal grown on Earth.