Extended Data Fig. 4: Electron density maps for AmpC–inhibitor complexes.
From: Ultra-large library docking for discovering new chemotypes
The initial Fo − Fc electron density map contoured at 2.5σ around the inhibitor (density in cyan) with refined 2Fo − Fc electron density contoured at 1σ for enzyme residues for the complexes with the following compounds. a, 547933290. b, 275579920. c, 339204163. d, 549719643. Inhibitor carbons are shown in cyan and enzyme carbons are shown in grey, oxygens in red, nitrogens in blue, sulfurs in yellow and chlorides in green.
