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A typical purple bacterial photosynthetic unit is composed of a reaction centre (RC) and two types of antenna complexes (LH1 and LH2). LH1 forms a stoichiometric complex with RC, called the RC/LH1 core complex, while LH2 antennas are arranged peripherally around the core. All of these pigmentprotein complexes are integral membrane proteins. High-resolution structures have been determined for both the RC alone and the LH2. So far however the best structural data on LH1 has come from an 8.5 Å projection map obtained from electron diffraction of 2D-crystal of LH1 from Rhodospir illum rubrum. We report here the structure of RC/LH1 core complex from R. palustris, which was isolated from membranes following solubilization with the LDAO. The complex was purified by a combination of ion exchange and molecular sieve chromatography, then for crystallization exchanged into 1% sucrose monocholate. Crystals were grown by vapor diffusion in presence of 10 nM MgCl2, 8% MMePEG2K and 1% spermidine. The 4.8 Å data were collected at 100 K (st.14.1, SRS Daresbury), and indexed in P1 (a = 76.04, b = 119.02, c = 130.43 Å, α = 69.3°, β = 72.7°, γ = 66.5°). 37283 reflections were measured with the average I/°s 7.5, completeness 97.4% and Rmerge 8.8%.

The crystal structure of the RC/LH1 complex fromRhodopseudomonas palustris