Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer

The membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. FBD in nanodiscs was found to be conformationally homogenous and enabled high-resolution NMR probing. P-31 NMR revealed the polymer's lack of preference for any specific E. coli lipids and identified the lipid-types in nanodiscs.

Automated summary

In this study, the membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. The FBD in nanodiscs showed conformational homogeneity and enabled high-resolution NMR probing. P-31 NMR revealed that the polymer had no preference for any specific E. coli lipids and identified the lipid types in the nanodiscs.