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. 2007 Dec 12;104(51):20280–20284. doi: 10.1073/pnas.0704599105

Fig. 1.

Fig. 1.

X-ray structure of the RC–LH1 complex from Rps. palustris (29). This structure was determined to a resolution of 4.8 Å. In this complex the RC is enclosed by the LH1, which features 15 αβ (purple and gray) apoproteins that are arranged in an overall elliptical shape and accommodate two BChl a molecules each. The positions and orientations of the BChl a molecules (red) were only placed in the model as guide for the eye. These positions were not absolutely determined at this resolution. The LH1 ring features a gap where one αβ dimer is replaced by another small protein (yellow) that has been termed W. The protein structure representation was prepared with VMD (36).