Supplementary Figure 1: Electron density of the Rpn11 catalytic active site in the apo and Zn2+-bound states. | Nature Structural & Molecular Biology

Supplementary Figure 1: Electron density of the Rpn11 catalytic active site in the apo and Zn2+-bound states.

From: Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation

Supplementary Figure 1

(a) The 2|Fo|-|Fc| electron density map of the Zn2+-bound active site is shown in grey and contoured at 1.5σ. Depicted in cyan is the |Fo|-|Fc| difference electron density map contoured at 5σ, calculated from the final coordinates after three rounds of ADP and reciprocal space XYZ refinement with the Zn2+ ion and the catalytic water omitted. (b) 2|Fo|-|Fc| electron density map of the Rpn11 active site in the apo state, contoured at 1.5σ. Also included is the corresponding |Fo|-|Fc| difference electron density map contoured at 5σ, which does not show any peaks at this contouring level.

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