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. Author manuscript; available in PMC: 2011 Aug 20.
Published in final edited form as: J Mol Biol. 2010 Jul 1;401(3):363–373. doi: 10.1016/j.jmb.2010.06.044

Figure 2. Projection maps of PDE6, PDE6-PrBP/δ and PDE6-PrBP/δ-GST complexes.

Figure 2

. Negatively stained PDE6 complexes exhibit an elongated shape with a wide top and a narrower end. Reproducible substructure is enhanced in the class averages shown in the inset, revealing two stain-filled cavities. B. Similar particles are observed in micrographs of PDE6-PrBP/δ preparations. Upon closer inspection, ~10% of these complexes show an additional domain protruding from the wider end (arrowheads). Even less frequently, two such domains are found to be attached. The selected class averages (inset) show that these protruding domains are emerging from a well-defined site, which is the putative location of isoprenylation in the catalytic domain (see also Figure 5). C. PDE6-PrBP/δ-GST complexes are significantly longer as result of the PrBP/δ-GST chimeric protein attached to the wider end (arrowhead). Class averages in the top row of the inset display PDE6-(PrBP/δ-GST)2 complexes, whereas the bottom row shows PDE6-PrBP/δ-GST complexes. D. Averages, standard deviation (SD) maps and difference maps from PDE6 and PDE6-PrBP/δ complexes. D1: PDE6; D2: SD of PDE6; D3: PDE6-PrBP/δ; D4: SD of PDE6-PrBP/δ; D5: PDE6-PrBP/δ – PDE6. The scale bars represent 150 Å; boxes of the insets have a width of 290 Å, and those in D are 250 Å wide.