Science Advances

This PDF file includes:

• Supplementary Materials and Methods
  
• Fig. S1. Overall domain alignment of copper-containing hydroxylases.
  
• Fig. S2. Sequence alignment of copper-containing hydroxylases.
  
• Fig. S3. Sequence alignment of DBH from different organisms.
  
• Fig. S4. Size exclusion analysis of purified DBH tetramer and dimer.
  
• Fig. S5. Analysis of DBH tetramer conversion as a function of pH.
  
• Fig. S6. Analysis of DBH tetramer conversion as a function of ionic strength.
  
• Fig. S7. Mass spectrum of a nonseparated sample containing a mixture of dimeric and tetrameric DBH.
  
• Fig. S8. SDS–polyacrylamide gel electrophoresis analysis of dimeric and tetrameric DBH under nonreducing and reducing conditions.
  
• Fig. S9. Structure of the human DBH dimer emphasizing the integrated structure created by the C-terminal interaction with both the Cu_M domain and the DOMON domain.
  
• Fig. S10. Modeled glycosylation environments in chain A with 2F_obs − F_calc electron density maps contoured at σ of 1.0.
  
• Fig. S11. Modeled glycosylation environments in chain B with 2F_obs − F_calc electron density maps contoured at σ of 1.0.
  
• Fig. S12. Structure of the human DBH dimer with the disulfide bridges and the glycosylation sites highlighted.
  
• Fig. S13. Sequence alignment of DOMON domains.
  
• Fig. S14. The dimerization domain disulfide bridges environment with 2F_obs − F_calc electron density map contoured at σ of 1.0.
  
• Table S1. Secondary structure assignment in human DBH.
  
• Table S2. Domain-domain hydrogen bond contacts in chains A and B.
  
• Table S3. Data collection, phasing, and refinement statistics.

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