The application of powder diffraction methods in two-dimensional crystallography is regarded as intractable because of the uncertainties associated with overlapping reflections. Here, we report an approach that resolves these ambiguities and provides reliable low-resolution phase information directly from powder diffraction data. We apply our method to the recovery of the structure of the bacteriorhodopsin (bR) molecule to a resolution of 7 angstroms using only powder diffraction data obtained from two-dimensional purple membrane (PM) crystals.
@article{arxiv.1007.0065,
title = {A novel approach for structure analysis of two-dimensional membrane protein crystals using x-ray powder diffraction data},
author = {Ruben A. Dilanian and Connie Darmanin and Jose N. Varghese and Steve W. Wilkins and Toshihiko Oka and Naoto Yagi and Harry M. Quiney and Keith A. Nugent},
journal= {arXiv preprint arXiv:1007.0065},
year = {2010}
}