The Mechanosensitive channel of Large conductance (MscL) in Escherichia coli is a protein channel primarily activated by membrane tension1 . As one of the most extensively studied membrane protein channels, it has become a prototype for the mechanically gated class of ion channels2 . However, there remains to date no high resolution protein structure for the E. coli channel, while the the structure of the activated channel has not been revealed for any organism. Obtaining this knowledge is critical not only from a pure science perspective, but also to aid the engineering of functional nanovalves based on MscL2 .
Here we present the latest results from our ongoing efforts to structurally and biochemically characterise MscL. Recent developments have focused on the production of improved MscL constructs for structural studies and ongoing lipid reconstitution experiments for single particle analysis and potentially 2D crystallography. In addition, optimal lipid environments that promote MscL stability and allow it to retain functionality have been investigated.