Science Advances

Supplementary Materials

This PDF file includes:

  • fig. S1. Same dimerization mode in Dscam1 Ig1-Ig49.44 with or without bivalent cations.
  • fig. S2. SPR measurement of Ig1-Ig49.44 homophilic binding.
  • fig. S3. Variability of the same Ig2 or Ig3 in different combinations.
  • fig. S4. Potential glycosylation sites on the variable parts of Dscam1 Ig2 and Ig3.
  • fig. S5. Context setting restrictions for protein recognition.
  • fig. S6. Purified Dscam1 proteins for crystallization.
  • table S1. X-ray data refinement statistics.
  • table S2. Intermolecular angles (°) of different Dscam1 Ig2-Ig3 isoforms.
  • table S3. Buried area (Å2) of the Dscam1 homodimer of Ig1-Ig4, Ig2, and Ig3.

Download PDF

Files in this Data Supplement: