The major light-harvesting complex of photosystem II (LHC-II) serves as the principal solar energy collector in the photosynthesis of green plants and presumably also functions in photoprotection under high-light conditions. Many of its structures were revealed by a work of a 3.2 A electron crystallographic model of LHC-II in 1994. Since then researchers have eagerly awaited a higher-resolution structure to extend knowledge of the light harvesting and energy transfer processes involved in photosynthesis to the level of full atomic data. In cooperation with a research team headed by Prof. Kuang Tingyun from the CAS Institute of Botany, a research group led by Prof. Chang Wenri of the CAS Institute of Biophysics has succeeded in determining the crystal structure of the complex, from spinach, by revealing the first X-ray structure of LHC-II in icosahedral proteoliposome assembly at atomic detail. The 14 chlorophylls in each LHC-II monomer are revealed as 8 chlorophyll a and 6 chlorophyll b molecules, and the position of each pigment in the complex has been accurately mapped at 2.72 A resolution.
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