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Microscopic and light spectroscopic investigations on the supramolecular architecture of bacterial photosynthetic membranes have revealed the photosynthetic protein complexes to be arranged in a densely packed energy-transducing network. Protein packing may play a determining role in the formation of functional photosynthetic domains and membrane curvature. To further investigate in detail the packing effects of like-protein photosynthetic complexes, we report an atomic force microscopy investigation on artificially created 2D crystals of the peripheral photosynthetic light-harvesting complexes 2 (LH2's) from the bacterium Rhodobacter sphaeroides. Instead of the usually observed one or two different crystallization lattices for one specific preparation protocol, we find seven different packing lattices. The most abundant crystal types all show a tilting of LH2. Most surprisingly, although LH2 is a monomeric protein complex in vivo, we find an LH2 dimer packing motif. We further characterize two different dimer configurations: in type 1, the LH2's are tilted inwards, and in type 2, they are titlted outwards. Closer inspection of the lattices surrounding the LH2 dimers indicates their close resemblance to those LH2's that constitute a lattice of zig-zagging LH2's. In addition, analyses of the tilt of the LH2's within the zig-zag lattice and that observed within the dimers corroborate their similar packing motifs. The type 2 dimer configuration exhibits a tilt that, in the absence of up-down packing, could bend the lipid bilayer, leading to the strong curvature of the LH2 domains as observed in Rhodobacter sphaeroides photosynthetic membranes in vivo.