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Atomic model of plant light-harvesting complex by electron crystallography

Nature volume 367, pages 614–621 (1994)Cite this article

Abstract

The structure of the light-harvesting chlorophyll a/b–protein complex, an integral membrane protein, has been determined at 3.4 Å resolution by electron crystallography of two-dimensional crystals. Two of the three membrane-spanning α-helices are held together by ion pairs formed by charged residues that also serve as chlorophyll ligands. In the centre of the complex, chlorophyll a is in close contact with chlorophyll b for rapid energy transfer, and with two carotenoids that prevent the formation of toxic singlet oxygen.

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Author information

Author notes

  1. Yoshinori Fujiyoshi: Protein Engineering Research Institute, 6-2-3, Furuedai, Suita, Osaka 565, Japan

Authors and Affiliations

  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117, Heidelberg, Germany

    Werner Kühlbrandt, Da Neng Wang & Yoshinori Fujiyoshi

Authors
  1. Werner Kühlbrandt
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  2. Da Neng Wang
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  3. Yoshinori Fujiyoshi
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Kühlbrandt, W., Wang, D. & Fujiyoshi, Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614–621 (1994). https://doi.org/10.1038/367614a0

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