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- W2048762603 abstract "When the light-harvesting chlorophyll a/b protein complex (LHC-II) from pea thylakoid membranes is co-crystallized with native lipids, an octahedral crystal that exhibits no birefringence is obtained. Cryogenic electron micrographs of a crystal edge showed the crystal to be made up of hollow spherical assemblies with a diameter of 250 A. X-ray diffraction data at 9.5 A resolution revealed the spherical shell of LHC-II to have icosahedral symmetry. A T = 1 icosahedral model of LHC-II, in which the stromal surface of the protein faces outward, was constructed using the previously reported structure of the LHC-II trimer [Kühlbrandt et al. (1994), Nature (London), 367, 614-621]. The present result shows the first example of a well ordered three-dimensional crystal of icosahedral proteoliposomes." @default.
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- W2048762603 date "2004-04-21" @default.
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- W2048762603 title "An icosahedral assembly of the light-harvesting chlorophyll<i>a</i>/<i>b</i>protein complex from pea chloroplast thylakoid membranes" @default.
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- W2048762603 doi "https://doi.org/10.1107/s0907444904003233" @default.
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