A light-harvesting siphonax-anthin-chlorophylla/b-protein complex of marine green alga,Bryopsis corticulans

2004 ◽  
Vol 49 (18) ◽  
pp. 1936-1941
Author(s):  
Hui Chen ◽  
Shihua Shen ◽  
Junfang He ◽  
Jing Leng ◽  
Liangbi Li ◽  
...  
2014 ◽  
Vol 123 (1) ◽  
pp. 61-76 ◽  
Author(s):  
Xiaochun Qin ◽  
Wenda Wang ◽  
Lijing Chang ◽  
Jinghua Chen ◽  
Peng Wang ◽  
...  

2020 ◽  
Vol 1861 (5-6) ◽  
pp. 148186
Author(s):  
Dan-Hong Li ◽  
Wenda Wang ◽  
Cuicui Zhou ◽  
Yan Zhang ◽  
Peng Wang ◽  
...  

2005 ◽  
Vol 83 (3) ◽  
pp. 297-305 ◽  
Author(s):  
Binxing Li ◽  
Dazhang Mao ◽  
Yulong Liu ◽  
Liangbi Li ◽  
Tingyun Kuang

Author(s):  
Werner Kühlbrandt ◽  
Da Neng Wang ◽  
K.H. Downing

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.


1992 ◽  
Vol 6 (4) ◽  
pp. 363-367 ◽  
Author(s):  
Osamu Takimura ◽  
Hiroyuki Fuse ◽  
Yukiho Yamaoka
Keyword(s):  

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