The supramolecular architecture of human heteromeric amino acid transporters unveiled by the Fotiadis Lab.
Please see our recent publication: Rosell et al. (2014), Proc. Natl. Acad. Sci. USA.
Welcome to the website of the Fotiadis Lab
Structural biology of membrane proteins
We investigate the structure and supramolecular organization of membrane proteins using high-resolution microscopy techniques, i.e. transmission electron microscopy (TEM) and atomic force microscopy (AFM), and X-ray crystallography.
Single particle analysis is used to determine the structure and oligomeric state of detergent-solubilized membrane proteins from projection images obtained by TEM.
Electron crystallography of 2D membrane protein crystals is applied to reveal the projection and 3D structure of membrane proteins embedded in the lipid membrane. To determine the topography and dynamics of membrane proteins, proteoliposomes and 2D crystals are imaged by AFM.
In 2006 we also started expanding to 3D crystallization and X-ray crystallography of membrane proteins.
Our mission is to assess the structure and supramolecular organization of membrane proteins in the detergent-solubilized state and in their native environment, the lipid bilayer.
Our target proteins consist mainly (but not only) of membrane transport and channel proteins.
Our research is founded by