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Institute of Biochemistry, ETH Zurich
My group is focusing on the structure and function of membrane proteins involved in signal transduction. We started using cryo-EM and single-particle analysis to study the structure of proteins of interest: the membrane adenylyl cyclases and their complexes with other signalling-related proteins. We were interested in acquiring cryo-EM data and decided to try data collection at EMBL with the support of the iNEXT programme.
In early 2018 we collected a high-resolution cryo-EM dataset at EMBL. This formed the basis of our study on the structure of the membrane adenylyl cyclase AC9 bound to a G protein alpha subunit. Using the data collected at EMBL, we were able to reconstruct the 3D structure of this important membrane protein complex at 3.4 Å resolution. The structure provided unique insights into the function of the membrane adenylyl cyclase complex. We were excited to publish our findings in Science in April 2019.
Access to the cryo-EM facility enabled our structural studies of relatively small and challenging membrane proteins, such as the adenylyl cyclases. Access to a facility that operates at such a high level and produces such high-quality cryo-EM datasets is a real asset to my research.
I think the people who work at this facility make it a unique place – in my opinion the expertise of the staff members at the EMBL cryo-EM facility, in particular Wim Hagen and Felix Weis, is simply outstanding. This translates into the highly professional operation of the facility, including instrument maintenance and operation, organisation of user access, sample handling, data acquisition, and data handling.
I would congratulate them on making the right choice – their project will be in the hands of the top experts in cryo-EM data acquisition.