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Figure 3
Difference electron-density maps of PK (a) and A2AAR [(b) and (c)] structures to illustrate the absence of model bias. Residue fragment Val226–Tyr236 of PK structure (a), Ile100–Leu110 of A2AAR (b) and ligand ZM241385 (c) were deleted from models and simulated-annealing OMIT maps 2mFo − DFc (gray) and mFo − DFc (green) were calculated. In all cases [(a) and (b)], OMIT maps 2mFo − DFc are contoured at 1.5σ and mFo − DFc are contoured at 2.5σ. Omitted residues are shown for clarity. The positive electron density, where original residues were, is in good agreement with the final structural model of PK and A2AAR.

IUCrJ
Volume 6| Part 3| May 2019| Pages 412-425
ISSN: 2052-2525
https://doi.org/10.1107/S205225251900263X