Extended Data Fig. 2: Comparison of the two molecules present in the asymmetric unit of SAMURI-ProSeDMA.
From: Structure and catalytic activity of the SAM-utilizing ribozyme SAMURI
a. Superimposition of the two molecules present in the asymmetric unit. b. The maximal distances between the molecules are located in the P1 stem with 9.6 and 5.5 Å at the 5′ and 3′ ends, respectively. This structural diversity correlates with the flexible location of the methionine moiety in the pocket (c). d. Zipper region connecting the bottom layer and P2. e. Electron density maps for the active site in the A molecule. Blue mesh represents the σA- weighted 2Fo-Fc map contoured at 1σ and positive difference density for the cofactor and the propargyl group is shown in green at a contour level of 3σ.
