Figure 1
From: Opportunistic complexes of E. coli L-asparaginases with citrate anions
The active site region of the EcAI(T162A). Protein residues are shown as sticks, the 2mFo-DFc maps contoured at 1·σ level are shown in orange, mFo-DFc maps contoured at 3·σ level are blue, with no significant negative density present at −3·σ level. (a) Omit map (mFo-DFc) for the re-refined model (PDB ID 6nxc) with Thr14, citrate, and several solvent molecules removed from phase calculations, superimposed on the final model. (b) The final 2mFo-DFc map for the re-refined structure, with no difference density remaining at +/−3·σ level. (c) Omit map for the original structure (PDB ID 2 him), calculated as in panel a), with the original coordinates superimposed. (d) The final maps calculated for the originally deposited model. A significant positive density is present in the difference map.
