An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes

Tomoya Hino, Eiji Kanamori, Jian Ren Shen, Tsutomu Kouyama

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

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 Å. X-ray diffraction data at 9.5 Å 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.

Original languageEnglish
Pages (from-to)803-809
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number5
DOIs
Publication statusPublished - May 1 2004
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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