Extended Data Fig. 4: Composite OMIT map of IbpATReNDCdc42 X-ray crystal structure.
From: Identification of targets of AMPylating Fic enzymes by co-substrate-mediated covalent capture
Electron density map covering the whole structure. b, Unbiased electron density map of TReND-1 as covalent linker. Electron density of phosphate atoms suggests an alternative conformation for the TReND-1 in the covalent ternary complex. The absence of adenine base allows the phosphate group and linked tyrosine 32 of Cdc42 to fill in space and adopt an alternative conformation, which is indicated as pink carbon atoms. Canonical conformation is indicated as light-green carbon atom. Electron density of tyrosine 32 is less resolved due to flexibility. OMIT map is constructed with sigma 1.0 and carve distance of 2 Å to the linker.
