Black-white space group

Fig. 8. (a) Structure of the full-length Rieske protein from bovine heart mitochondrial bci complex. The catalytic domain is connected to the transmembrane helix by a flexible linker, (b) Superposition of the three positional states of the catalytic domain of the Rieske protein observed in different crystal forms. The ci state is shown in white, the intermediate state in gray, and the b state in black. Cytochrome b consists of eight transmembrane helices and contains two heme centers, heme and Sh-Cytochrome c i has a water-soluble catalytic domain containing heme c i and is anchored by a C-terminal transmembrane helix. The heme groups are shown as wireframes, the iron atoms as well as the Rieske cluster in the three states as space-filling representations. 

Figure E.4. Cross-eye stereo view of the Fj-motor of ATP synthase with y-rotor in ribbon and E and C chains in space-filling representation with residues indicated as neutral in light gray, aromatic in black, other hydrophobics in gray, and charged in white. Lines indicate a repulsive interaction (i.e., AG,p) between the hydrophobic y-rotor and SO4 (in place of hydrolyzed y-phosphate) and augmented by newly emerged charged groups that occurs in the Pe chain.

Fig. 1. Space-filling drawing of yeast iso-l-cytochrome c (see Ref. 19). Atoms coloured black form a part of the heme prosthetic group (shown exposed alongside). Atoms coloured grey (arrowed) belong to lysine and arginine side chains on the protein surface. Atoms coloured white represent those not falling into either of these categories. This illustration was kindly provided by Michael Murphy and Gary Brayer (University of British Columbia)...

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