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Cryst Growth Des. 2017 Jun 7;17(6):3502-3511. doi: 10.1021/acs.cgd.7b00458. Epub 2017 May 12.

Chemically Stable Lipids for Membrane Protein Crystallization.

Author information

1
Department of Chemistry, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.
2
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
3
Laboratory for Advanced Studies of Membrane Proteins, Moscow Institute of Physics and Technology (MIPT), Dolgoprudny, Russia.
4
Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, Russia.
5
Laboratory for Structural Biology of GPCRs, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
6
Institute of Complex Systems (ICS-6): Structural Biochemistry, Research Centre Jülich, Germany.

Abstract

Lipidic cubic phase (LCP) has been widely recognized as a promising membrane-mimicking matrix for biophysical studies of membrane proteins and their crystallization in a lipidic environment. Application of this material to a wide variety of membrane proteins, however, is hindered due to a limited number of available host lipids, mostly monoacylglycerols (MAGs). Here, we designed, synthesized and characterized a series of chemically stable lipids resistant to hydrolysis, with properties complementary to the widely used MAGs. In order to assess their potential to serve as host lipids for crystallization, we characterized the phase properties and lattice parameters of mesophases made of two most promising lipids at a variety of different conditions by polarized light microscopy and small-angle X-ray scattering. Both lipids showed remarkable chemical stability and an extended LCP region in the phase diagram covering a wide range of temperatures down to 4 °C. One of these lipids has been used for crystallization and structure determination of a prototypical membrane protein bacteriorhodopsin at 4 °C and 20 °C.

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