Fig. 4: Structural dynamics of ADAR1 dimer in the absence of substrate dsRNA.
From: High-speed atomic force microscopy and 3D modeling reveal the structural dynamics of ADAR1 complexes
a HS-AFM observations indicated that ADAR1 monomers interact with each other, and the distance between two monomers in the dimer fluctuates with flexible and dynamic N-terminal domain regions. b Peak-to-peak distance between monomers fluctuates, as shown by the cross-sectional analysis of the dimers. c The schematic drawing represents the distance range of fluctuations between two monomers in a dimer. Imaging parameters: scanning area = 100 × 100 nm2 (100 × 80 pixels); frame rate = 3.3 frames/s. The displayed area is 57 × 59 nm2. Representative data from more than 3 independent experiments with similar results are shown. Source data of the graphs are provided as a Source Data file.
