Obtaining well ordered crystals of membrane proteins is the single most ser
ious stumbling block in the pursuit of their high-resolution structures. Th
e applicability of lipidic cubic phase-mediated crystallization is demonstr
ated on a diverse set of bacterial membrane proteins: two photosynthetic re
action centres, a light-harvesting complex and two retinal proteins, halorh
odopsin and bacteriorhodopsin. Despite marked differences in molecular dime
nsions, subunit composition and membrane origin, one single lipid, monoolei
n, is sufficient to form a crystallization matrix for all the aforementione
d systems. Therefore, the lipidic cubic phase approach is proposed as a gen
eral method for crystallizing membrane proteins.