Nuclear Magnetic Resonance Facility
The NMR facility is located at the Vienna Biocenter in building VBC5 in the Department of Structural and Computational Biology of the University of Vienna. It currently houses a 500, two 600 and an 800MHz spectrometer. In addition, the unit also has IT facilities for structure calculations, molecular visualisation and data analysis. Its mission is to use state-of-the-art NMR spectroscopy and to apply it to biological problems. We offer a full range of NMR research services from routine sample characterisation to determination of solution structures of biological macromolecules. NMR also works together with other techniques in structural biology, especially X-ray crystallography, which is also available in-house, thus using an integrated approach to the determination of biological structure and function. We do this in collaboration with our colleagues from the Max F. Perutz Laboratories, the Vienna Biocenter and beyond.
VBC 5 - Level E1 - Room 1.608
The usage of this facility is not restricted to MFPL only; in principle it is also open to other customers. However, it must be noted that samples submitted from MFPL will always have priority, and samples submitted by other institutions will only be analyzed according to capacity. Pricing depends on the number of samples and the type of analysis: please contact us for further information.
Authorized users can reserve the facility via the MFPL intranet. All external users should contact the Facility Manager directly for a quotation.
By using the NMR faclilty you agree to our terms of business (here)
We operate a series of research infrastructure entities, consisting of high-end technical instrumentation. We offer up-to-date methodology and modern equipment.
The usage of our infrastructure is open to external users, provided that we can offer free capacities. Please contact us to inquire about our research services and fees.
By using the NMR facility you agree to our terms of business (here)
NMR determination of the binding site and binding mode of a natural ligand to its protein target: A 15N-HSQC spectra of a siderocalin protein Q83 (B) in the absence (blue peaks) and in the presence (red peaks) of a ligand molecule Enterobactin (C) Mapping of the shifted peaks (in red) onto the (known) protein structure clearly reveals a defined binding site (B) (unpublished results)
Scientific Steering Committee
Kristina Djinovic-Carugo Group Leader
kristina.djinovic [AT] univie.ac [DOT] at
Robert Konrat Group Leader
robert.konrat [AT] univie.ac [DOT] at
Renée Schroeder Group Leader
renee.schroeder [AT] univie.ac [DOT] at
Tim Skern Group Leader
timothy.skern [AT] muv.ac [DOT] at