Supplementary Figure 2: Experimental and anomalous electron density maps.
From: Structure of the active form of Dcp1–Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator
A. Experimental electron density map (contour: 1σ) obtained by Se-MAD. The m7GDP molecule bound to Dcp2 active site is shown in red sticks. Color code is the same as for Fig.1A.
B. Anomalous difference electron density map (contour: 4σ) calculated from the dataset collected at the energy corresponding to the peak of Se absorption spectra, showing the location of Se atoms from selenomethionines. The methionine side chains as built in the final model are shown as sticks, validating side chain assignment in our structure.
