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![[Figure 3]](ap5048fig3mag.jpg)
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Figure 3
Comparison between the electron density recovered from SSX studies using a flow cell and SFX studies using a high-viscosity injector. (a) 2Fobs − Fcalc electron density map (blue, contoured at 1.5σ) showing SSX electron density for the active site heme a3 of ba3-type CcO determined at 2.12 Å resolution recovered using the flow cell for sample injection. (b) 2Fobs − Fcalc electron density map (blue, contoured at 1.5σ), showing SFX electron density for the active site heme a3 at 2.3 Å resolution recovered using a high-viscosity injector for sample injection (Andersson et al., 2017  ). (c) 2Fobs − Fcalc electron density map (blue, contoured at 1.0σ) showing SSX electron density for a representative glutamic acid residue within the protein. (d) 2Fobs − Fcalc electron density map (blue, contoured at 1.0σ) showing SFX electron density for a representative glutamic acid residue within the protein. (e) Fobs − Fcalc omit electron density map (green, contoured at 4.5σ), showing a slightly elongated electron density in the active site of the SSX structure. (f) Fobs − Fcalc omit electron density map (green, contoured at 4.5σ) showing a slightly more spherical electron density in the active site of the SFX structure (Andersson et al., 2017). For both omit maps the electron density map is calculated without modelling any ligand between the heme a3 iron and CuB. |
![[Figure 3]](ap5048fig3.jpg)
 | JOURNAL OF APPLIED CRYSTALLOGRAPHY |
ISSN: 1600-5767
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