Lipid Chemistry

A more stable phase via triangulation

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Science  16 Jan 2015:
Vol. 347, Issue 6219, pp. 245
DOI: 10.1126/science.347.6219.245-g

Bacteriorhodopsin, which can be crystalized ex-vivo at low temperatures


Cell membranes house many important proteins that are hard to study outside their native environment. Salvati Manni et al. now have devised a special building block that stabilizes artificial, membrane-like phases at low temperature. Their approach potentially opens the door to more detailed studies of temperature-sensitive membrane proteins. Biological membranes assemble from lipid molecules. The authors induced low-temperature stability by incorporating a rigid triangular ring, or cyclopropyl group, into a more conventional lipid structure. They validated the result by x-ray analysis of embedded bacteriorhodopsin protein at 4°C.

Angew. Chem. Int. Ed. 10.1002/anie.201409791 (2014).

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