First structure of an SLC16 family transporter homologue with bound substrate and inhibitor.
Please see our recent publication: Bosshart et al. (2019), Nature Commun.
The Fotiadis Lab
Want to learn about the Fotiadis Lab and its research ?
Please see our publication in International Innovation (2013).
Welcome to the website of the Fotiadis Lab
Structure and function of membrane proteins
We investigate the structure and function of membrane proteins with a special focus on membrane transport proteins. The methods of choice are high-resolution microscopy techniques (electron and atomic force microscopy) and X-ray crystallography.
Our methods of choice for the structure determination of membrane proteins are electron microscopy and X-ray crystallography. In addition atomic force microscopy is used to image membrane proteins embedded in lipid bilayers under near-physiological conditions.
Our mission is to assess the structure and function of membrane proteins in the detergent-solubilized state and in their native environment, the lipid bilayer.
Our target membrane proteins consist mainly of membrane transport proteins and receptors.
Latest Tweets from FotiadisLab @IBMM_UniBE
July 7, 2021:
Please check out our latest publication:
Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin
Congratulations to all authors and a special "thank you" to Stephan (UniBE) and Thomas (UniZH/ETHZ) !!!
June 16, 2021:
Open Postdoc position in the FotiadisLab (Bern, Switzerland):
In structural characterization of viral and membrane proteins by cryo-electron microscopy
For details, please see:
January 27, 2021:
Open positions at the FotiadisLab
Ph.D. student position:
Are you interested in membrane proteins biochemistry, function and structure ?
We are looking for researchers to join our team !
October 19, 2020:
Please check out our newest publication on the effects of the ancillary protein 4F2hc on the substrate affinity and specificity of the human transporters LAT1 and LAT2.
Great work by Satish and colleagues, congratulations !
October 12, 2020:
Our first contribution to Coronavirus research.
An excellent collaboration with Thomas Lemmin (ETH Zurich/University of Zurich) and Philippe Plattet (Vetsuisse, University of Bern) – thank you !
October 1, 2020:
One step further...
Please check out Jean-Marc’s new publication entitled: “Sub-Nanometer Cryo-EM Density Map of the Human Heterodimeric Amino Acid Transporter 4F2hc-LAT2”.
Excellent job !
September 29, 2020:
Please discover our new double-chambered device for macromolecular crystal flash-cooling in different cryogenic liquids by Jeckelmann et al.
Congratulations Jean-Marc !
August 26, 2020:
Great review by Patrick Bosshart (@bossi1983) and colleagues (@MouseTransLab, @AvedaSci, @SchlessingerLab, @IBMM_UniBE) on SLC16 family transporters. Congrats !
August 19, 2020:
Very happy that we: Philippe Plattet (Uni Bern), Markus Seeger (Uni Zurich) and I (Uni Bern) received one of the 28 new Coronavirus grants funded by the National Research Programme COVID-19.
Thanks to this funding, we will be able to contribute in the fight against Coronavirus.
August 13, 2020:
Want to produce engineered versions of 2D bacteriorhodopsin crystals (purple membranes) for basic research and applied technologies ?
Then, please check out our recent publication in Methods Protoc.: https://pubmed.ncbi.nlm.nih.gov/32707904/
Thank you Mirko and colleagues for the great job!
March 26, 2020:
Check out our latest publication within the NCCR Molecular Systems Engineering:
Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly
Congratulations Stephan !
March 4, 2020:
Check out our latest publication:
Cryo-EM structure of the prefusion state of canine distemper virus fusion protein ectodomain
Congratulations David !
June 14, 2019:
First structure of an SLC16 solute carrier family transporter with bound L-lactate and inhibitor: www.nature.com/articles/s41467-019-10566-6
Thank you and congratulations Patrick, David and Sara - you did a great job !
Our research is founded by