The use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.

ABSTRACT: Despite the great progress recently made in resolving their structures, investigation of the structural biology of membrane proteins still presents major challenges. Even with new technical advances such as lipidic cubic phase crystallisation, obtaining well-ordered crystals remains a significant hurdle in membrane protein X-ray crystallographic studies. As an alternative, electron microscopy has been shown to be capable of resolving >3.5Å resolution detail in membrane proteins of modest (~300 kDa) size, without the need for crystals. However, the conventional use of detergents for either approach presents several issues, including the possible effects on structure of removing the proteins from their natural membrane environment. As an alternative, it has recently been demonstrated that me

SUBMITTER: Postis V 

PROVIDER: S-EPMC4331651 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature