Neutron small angle scattering of matched proteoliposomes with incorporated F0F1 ATPase complex from Rhodospirillum rubrum FR1. An approach to the structure of membrane proteins in their natural environment.

Purified F0F1 ATPase from Rhodospirillum rubrum FR1 has been incorporated into lipid vesicles from the partially deuterated phospholipid dimyristoylglycerophosphocholine (DMPC-D54). These proteoliposomes were able to carry out energy transducing reactions. The incorporation of the membrane protein was controlled by freeze fracture electron microscopy. A method for structural research of the membrane protein in its natural environment has been developed by means of neutron small angle scattering. Using the contrast variation technique, the lipid part of the proteoliposomes was matched by adding an appropriate amount of D2O to the solvent. Thus the neutron scattering profile of F0F1 ATPase incorporated into vesicles was separated from the neutron scattering of the liposome. F0F1 ATPase incorporated in a lipid bilayer, as well as the free enzyme, yields a radius of gyration of Rg = 6.0 +/- 0.1 nm which leads to an overall diameter of 15.5 nm. This result suggests that the monomeric form of F0F1 ATPase is incorporated in DMPC-D54 membranes at 20 degrees C.