X-ray diffraction studies of human erythrocyte membrane structure.

Small angle x-ray diffraction patterns have been obtained from ordered arrays of hemoglobin-free human erthyrocyte membranes by use of improved techniques. Diffraction data have been recorded to 9 A resolution on samples whose lattice periodicity was varied (by changing humidity) from 55.5 A to 69.6 A. The observed reflections permitted tracing the intensity transform of the membranes. Phases for the reflections were assigned by the minimum wavelength principle. An electron density profile was then obtained by Fourier inversion, and yielded a symmetric membrane about 55 A in width. This structure can account for the previously reported diffuse scattering observed in other preparations (thus rendering unnecessary the proposed assignment of this scattering to a separated lipoprotein phase) and for the continuous scattering that we have recorded from isolated membranes in buffer. Lower resolution data that we have obtained from ultracentrifugally prepared lattices in buffer (and therefore without dehydration) are consistent with the above results, and support our view that we are observing diffraction from intact membranes.