| 研究実績の概要 |
The protein of interest (adenosine deaminase acting on dsRNA 2, ADAR2) has been successfully characterized in complex with two target dsRNA sequences by cryoEM. To accomplish this, roughly 300,000 particles extracted from 9300 micrographs containing ADAR2:GLI-61bp complex or 225,000 particles extracted from 15,000 micrographs were averaged together. Deaminase and double-stranded RNA binding domains were elucidated to 4-3.5-angstrom resolution, while RNA resolution varied from 6-3.5 angstroms. At the current resolution, cryoEM reconstructions are sufficient to elucidate the locations of deaminase domains and dsRBDs. Although density is not observed for all dsRBDs, novel interactions between protein and RNA can be hypothesized.
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