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It has proved difficult to obtain well diffracting single crystals of macromolecular complexes rich in lipid. We report here the path that has led to crystals of the bacteriophage PRD1, a particle containing approximately 2,000 protein subunits from 18 different protein species, around 10 of which are integral membrane proteins associated with a host-derived lipid bilayer of some 12,500 lipid molecules. These crystals are capable of diffracting X-rays to Bragg spacings below 4A. It is hoped that some lessons learned from PRD1 will be applicable to other lipidic systems and that these crystals will allow, as a proof of principle, the determination of the structure of the virus in terms of a detailed atomic model.

Type

Journal article

Journal

J Struct Biol

Publication Date

08/2002

Volume

139

Pages

103 - 112

Keywords

Bacteriophage PRD1, Bacteriophages, Cell Membrane, Crystallography, X-Ray, DNA, Viral, Electrophoresis, Polyacrylamide Gel, Lipid Bilayers, Lipid Metabolism, Lipids, Open Reading Frames, Salmonella enterica, Scattering, Radiation