Extended Data Fig. 6: Quality control and electron density maps for human phospho-parkin–phospho-ubiquitin.
a, LC–MS spectrum of crystallized human phospho-parkin (amino acids 1–382) bound to phospho-ubiquitin. This is representative of two independent experiments. b, Composite omit map (generated with simulated annealing) shown for the single complex in the asymmetric unit. 2|Fo|−|Fc| electron density is shown at 1σ. c, Electron density as in b for the Ubl–UPD linker. d, Electron density as in b for the Ser65 phospho-Ubl binding site on the UPD linker. e, Electron density as in b for the Ser65 phospho-Ub binding site. As we are missing electron density for disordered regions in the Ubl–ACT and ACT–UPD linkers, we cannot exclude the possibility that phospho-Ubl may interact in trans with a neighbouring parkin molecule. Also see Extended Data Table 1.
