This study describes the use of brominated phospholipids to distinguish between
lipid and detergent binding sites on the surface of a typical alpha-helical
membrane protein. Reaction centers isolated from Rhodobacter sphaeroides were
cocrystallized with added brominated phospholipids. X-ray structural analysis of
these crystals has revealed the presence of two lipid binding sites from the
characteristic strong X-ray scattering from the bromine atoms. These results
demonstrate the usefulness of this approach to mapping lipid binding sites at
the surface of membrane proteins.