Figure 4
From: Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature
Comparison of active site electron densities. (a–c) Fo-Fc omit map densities (green) contoured at 4.5 σ, calculated without any active site ligands. (a) The omit map density of ba 3 CcO from SFX data. The bound water molecule/hydroxide ion is shown in red. (b) The omit map density of ba 3 CcO from cryo-LCP data (PDB code 3S8G). The bound peroxide molecule is shown in red. (c) The omit map density of bovine heart aa 3-type CcO from XFEL data of large crystals at cryo temperature (PDB code 3WG7). Two bound peroxide molecules with partial occupancies are shown in red. (d–f) Fo-Fc difference densities calculated with a water molecule bound in the active site are shown in green (positive) and red (negative), contoured at +4.0/−4.0 σ. The bound water molecules are shown in red. (d) The Fo-Fc density of ba 3 CcO from SFX data. (e) The Fo-Fc density of ba 3 CcO from cryo-LCP data (PDB code 3S8G). (f) The Fo-Fc density of bovine heart aa 3-type CcO from XFEL data of large crystals at cryo temperature (PDB code 3WG7).
