Extended Data Fig. 8: Additional features of the SenDRT9 hexamer visualized by cryo-EM.
From: Protein-primed homopolymer synthesis by an antiviral reverse transcriptase
a, Local resolution map of the SenDRT9 RT-ncRNA hexamer (FSC cutoff 0.143), showing that resolution falls off near the periphery of the complex in flexible regions such as SL3 and SL4. b, Semi-transparent density highlighting a network of protein-RNA interactions that stabilize SL5. c, Semi-transparent density highlighting protein-protein interactions that stabilize the back-to-back assembly of trimers. d, Difference map generated by subtracting a calculated map of the model from the experimental density. Unmodelled density (grey) is visible in the map directly adjacent to the YADD active site (red), which may correspond to a small stretch of poly-dA product; repeated efforts to sort these particles failed to separate distinct conformational states. e, A close-up view of the SenRT active site (YADD residues in red). Density for the RT is shown as a semi-transparent surface, and the density map for the ncRNA is omitted here for simplicity. f, Semi-transparent density map highlighting the ncRNA poly-G track (residues 80-86) that was used to establish register for ModelAngelo.
