University of Eastern Finland Infrastructure for Native Mass Spectrometry
Finnish Infrastructure for Integrative Structural Biology is formed by three Centers of Excellence at the Universities of Helsinki, Oulu and Eastern Finland. We provide expert-supported access to services and technologies in sample preparation, characterization, and structure determination. The Finnish structural biology community is represented by the national consortium Instruct-FI, which is forming a national link to the Instruct-ERIC.
University of Eastern Finland (UEF) provides services and expertise in intact protein characterization with high-resolution native mass spectrometry techniques. The services include basic protein characterization (sequence verification, PTM analysis), analysis of protein folding and dynamics, and protein-ligand, protein-metal-ion and protein-protein interaction studies. The facility houses two state-of-the-art high-resolution instruments, a 12-T Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer (Bruker Solarix XR) and a trapped ion mobility time-of-flight mass spectrometer (Bruker timsTOF).
The unit is also one of the technology platforms of Biocenter Kuopio (BCK).
University of Eastern Finland is currently available for remote access, as well as physical visits by national scientists. Receiving international visitors is not currently possible due to COVID-19 restrictions. For information on the availability of specific technologies, view the Technology Availability List or contact firstname.lastname@example.org. Please check here regularly for updates.
How to find us
University of Eastern Finland services are located at the Department of Chemistry in Joensuu campus (Yliopistokatu 7, Futura building). The site is located near the city centre and can be reached from the local airport by taxi or a city bus (10 km).
UEF core facility offers two state-of-the-art mass spectrometers for versatile utilization of native mass spectrometry for studies of protein folding and assembly of biological macromolecules as well as for quantitative biological interaction studies with large dynamic range.