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The application of powder diffraction methods in two-dimensionalcrystallography is regarded as intractable because of the uncertaintiesassociated with overlapping reflections. Here, we report an approach thatresolves these ambiguities and provides reliable low-resolution phaseinformation directly from powder diffraction data. We apply our method to therecovery of the structure of the bacteriorhodopsin (bR) molecule to aresolution of 7 angstroms using only powder diffraction data obtained fromtwo-dimensional purple membrane (PM) crystals.

A novel approach for structure analysis of two-dimensional membrane protein crystals using x-ray powder diffraction data