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From:
Published online 2010 February 18. doi: 10.1107/S0108767309054361

Figure 3

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Structural results from intermediate trapping studies of bacteriorhodopsin. Four structures of resting (Belrhali et al., 1999 [triangle]) (purple, Protein Data Bank entry 1qhj), early (Edman et al., 1999 [triangle]) (blue, 1qkp), intermediate (Royant et al., 2000 [triangle]) (green, 1eop) and late (Luecke et al., 1999 [triangle]) (yellow, 1c8s) conformations are shown. These intermediate conformations were trapped by illuminating crystals at 110 K, 170 K and during thawing, respectively. A clear evolution of the retinal can be observed for these structures, which moves towards the cytoplasm as the temperature is raised. Moreover, significant displacements of Trp-182, Asp-85 and Arg-82 are also observed, as are rearrangements of water molecules recorded in the corresponding Protein Data Bank entries (not shown for reasons of clarity).

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