Cytochrome b5 was reconstituted with a highly deuterated phospholipid to form ordered multilayers consisting of repeated centrosymmetric pairs of asymmetric lipid-protein bilayers. Lamellar neutron diffraction data were collected to approximately 29 A resolution, and have been interpreted using models for the interaction of the membrane-binding domain of cytochrome b5 with the lipid bilayer. A range of different models was examined, and those in which the protein penetrates well into the bilayer, possibly spanning it, are favored. © 1983, The Biophysical Society. All rights reserved.
Gogol, E. P., Engelman, D. M., & Zaccai, G. (1983). Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayers. Biophysical Journal, 43(3), 285–292. https://doi.org/10.1016/S0006-3495(83)84352-5