Direct localization of detergents and bacteriorhodopsin in the lipidic cubic phase by small-angle neutron scattering.

ABSTRACT: Lipidic cubic phase (LCP) crystallization methods have been essential in obtaining crystals of certain membrane proteins, particularly G-protein-coupled receptors. LCP crystallization is generally optimized across a large number of potential variables, one of which may be the choice of the solubilizing detergent. A better fundamental understanding of the behavior of detergents in the LCP may guide and simplify the detergent selection process. This work investigates the distribution of protein and detergent in LCP using the membrane protein bacteriorhodopsin (bR), with the LCP prepared from highly deuterated monoolein to allow contrast-matched small-angle neutron scattering. Contrast-matching allows the scattering from the LCP bilayer itself to be suppressed, so that the distribution and be

SUBMITTER: Cleveland Iv T 

PROVIDER: S-EPMC7792994 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature