Specific association of photosystem II and light-harvesting complex II in partially solubilized photosystem II membranes.
In this study, we report the structural characterization of photosystem II complexes obtained from partially solubilized photosystem II membranes. Direct observation by electron microscopy, within a few minutes after a mild disruption of the membranes with the detergent n-dodecyl-alpha,D-maltoside, revealed the presence of several large supramolecular complexes. Images of these complexes were subjected to multivariate statistical analysis and classification procedures, resolving a new complex consisting of the previously characterized dimeric supercomplex of photosystem II and light-harvesting complex II [Boekema et al., Proc. Natl. Acad. Sci. USA 92 (1995) 175-179] and two additional, symmetrically organized protein masses each containing a second type of trimeric light-harvesting II complex. We conclude that large and labile integral membrane proteins, such as photosystem II, can be quickly structurally characterized without extensive purification.
Boekema
E J
EJ
Department of Biophysical Chemistry, BIOSON Research Centre, University of Groningen, The Netherlands.
van Roon
H
H
Dekker
J P
JP
D008565:Membrane Proteins; D008566:Membranes / Q000378:metabolism / Q000648:ultrastructure; D008854:Microscopy, Electron; D015999:Multivariate Analysis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000648:ultrastructure*; D045332:Photosystem II Protein Complex; D018724:Spinacia oleracea
D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex