TY - JOUR
T1 - Three-dimensional electron microscopy of the photosystem II core complex
AU - Mayanagi, Kouta
AU - Ishikawa, Takashi
AU - Toyoshima, Chikashi
AU - Inoue, Yorinao
AU - Nakazato, Katsuyoshi
N1 - Funding Information:
We thank Dr. Nakasako for discussions and Dr. K. Yonekura and Mr. K. Tani for their help in image analysis. This work was done with the support of the Special Postdoctoral Researchers Program of RIKEN (to K.M. and T.I.) and of PRESTO (to K.N.).
PY - 1998/11
Y1 - 1998/11
N2 - A three-dimensional image of the spinach photosystem II core complex composed of CP47, D1, D2, cytochrome b-559, and psbI gene product was reconstructed at 20-Å resolution from the two-dimensional crystals negatively stained with phosphotungstate. Confirming the previous proposal, the crystal had a p22121 symmetry. One PSH core complex was measured to be 80 x 80 Å in the membrane plane and 88 Å normal to it. The mass distribution was asymmetric about the lipid bilayer, consistent with predictions from the amino acid sequences. The lumenal mass consisted of three domains forming a characteristic triangular platform with another domain on top of it. Three stromal domains were smaller and linearly arranged. Due to strong stain exclusion in the hydrophobic core part of the lipid bilayer, the transmembrane region appeared to be imaged with a reversed contrast. Inverting the contrast resulted in a reasonable density distribution for that part. Thus, though the information on the transmembrane region is limited, the domain structure of the PSII core complex was revealed and allowed us to propose a model for the arrangement of subunits in the PSII core complex.
AB - A three-dimensional image of the spinach photosystem II core complex composed of CP47, D1, D2, cytochrome b-559, and psbI gene product was reconstructed at 20-Å resolution from the two-dimensional crystals negatively stained with phosphotungstate. Confirming the previous proposal, the crystal had a p22121 symmetry. One PSH core complex was measured to be 80 x 80 Å in the membrane plane and 88 Å normal to it. The mass distribution was asymmetric about the lipid bilayer, consistent with predictions from the amino acid sequences. The lumenal mass consisted of three domains forming a characteristic triangular platform with another domain on top of it. Three stromal domains were smaller and linearly arranged. Due to strong stain exclusion in the hydrophobic core part of the lipid bilayer, the transmembrane region appeared to be imaged with a reversed contrast. Inverting the contrast resulted in a reasonable density distribution for that part. Thus, though the information on the transmembrane region is limited, the domain structure of the PSII core complex was revealed and allowed us to propose a model for the arrangement of subunits in the PSII core complex.
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U2 - 10.1006/jsbi.1998.4033
DO - 10.1006/jsbi.1998.4033
M3 - Article
C2 - 9878576
AN - SCOPUS:0032214571
SN - 1047-8477
VL - 123
SP - 211
EP - 224
JO - Journal of structural biology
JF - Journal of structural biology
IS - 3
ER -