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Image: Magnus Andersson

Magnus P Andersson Lab

Research group We develop synchrotron-based time-resolved X-ray solution scattering methodology and studies protein dynamics in (mostly) membrane proteins.

The Magnus P Andersson research group develops synchrotron-based time-resolved X-ray solution scattering methodology to enable the study of membrane protein dynamics in real time. The focus is on ATP-dependent ion transporters with relevance in heart- and skeletal muscle disease, and for development of new antibiotics. We also use cryo-electron microscopy – both with conventional and time-resolved methods, and molecular dynamics simulations, which form the fundament for developing tools to handle and understand synchrotron data.


Cardiovascular disease

Calcium transport across cellular membranes is central to the beating of the heart. Contraction is achieved by calcium flooding the cell and to enable relaxation that calcium must be transported back to its storage compartment. The back-transport of calcium is carried out by an ATP-dependent membrane protein that we refer to as SERCA. We have used out developed synchrotron-based time-resolved X-ray solution scattering methodology to determine structures and kinetics of transition states in the SERCA reaction that are difficult or impossible to study with alternative biophysical techniques. We now use this method to study regulation mechanisms by e.g. lipids, pharmaceuticals, and internal protein domains. The goal is to gain molecular control of calcium signalling and thereby mitigate e.g. heart failure.    

Because calcium signalling also is a primary stress response in plants, we are also developing strategies to reduce this stress response on a molecular level. The goal of this particular approach of our research is to optimize crop yields and quality, which is critical given ongoing climate change to help achieve food security.

Infection biology

ATP-dependent membrane proteins that export heavy metals are central to bacterial survival and are therefore prime targets for developing new antibiotics. We focus on bacterial zinc transport in Shigella sonnei where the same protein is missing in human – which further increases its relevance as a target protein for development of new antibiotics. 


Publications since 2020

Orädd, F., Steffen, J.H., Gourdon, P., Andersson, M. Copper binding leads to increased dynamics in the regulatory N-terminal domain of full-length human copper transporter ATP7B. PLoS Computational Biology. 18(9):e1010074, (2022).

Salustros, N., Grønberg, C., Abeyrathna, N.S., Lyu, P., Orädd, F., Wang, K., Andersson, M., Meloni, G., Gourdon, P. Structural basis of ion-uptake in P1B-type ATPases. Nature Communications. 13(1):1-11, (2022).

Wiuf, A., Steffen, J.H., Becares, E.R., Grønberg, C., Mahato, D.R., Rasmussen, S.G.F., Andersson, M., Croll, T.,  Gotfryd, K., Gourdon, P. The two-domain elevator-type mechanism of zinc-transporting ZIP proteins. Science Advances. 8(28):eabn4331, (2022).

Li P., Nayeri, N., Górecki, K., Becares, E.R., Wang, K., Mahato, D.R., Andersson, M., Abeyrathna, S.S., Lindkvist‐Petersson, K., Meloni, G., Missel, J.W., Gourdon, P. PcoB is a defense outer membrane protein that facilitates cellular uptake of copper. Protein Science. 31(7):e4364, (2022).

Gronberg, C., Hu, Q., Mahato, D.R., Longhin, E., Salustros, N., Duellli, A., Lyu, P., Bågenholm, V., Eriksson, J., Rao, K.U., Henderson, D.I., Meloni, G., Andersson, M., Croll, T., Godaly, G., Wang, K., Gourdon, P. Structure and ion-release mechanism of PIB-4-type ATPases. Elife. 10:e73124, (2021).

Ygberg, S., Akkuratov, E.E., Howard, R.J., Taylan, F., Jans, D.C., Mahato, D.R., Katz, A., Kinoshita, P.F., Portal, B., Nennesmo, I., Lindskog, M., Karlish, S.J.D., Andersson, M., Lindstrand, A., Brismar, H., Aperia, A. A missense mutation converts the Na+,K+-ATPase into an ion channel and causes therapy-resistant epilepsy. Journal of Biological Chemistry. 297(6):101355, (2021).

Orädd, F., Ravishankar, H., Goodman, J., Rogne, P., Backman, L., Duelli, A., Pedersen, M.N., Levantino, M., Wolff, M., Wolf-Watz, M., Andersson, M. Tracking the ATP-binding response in adenylate kinase in real time. Science Advances. 7(47):eabi5514, (2021).

Orädd, F., Andersson, M. Tracking membrane protein dynamics in real time. Journal of Membrane Biology. 254:51-64, (2021).

Ravishankar, H., Pedersen, M.N., Eklund, M., Sitsel, A., Li, C., Duelli, A., Levantino, M., Wulff, M., Barth, A., Olesen, C., Nissen, P., Andersson, M. Tracking Ca2+ ATPase intermediates in real-time by X-ray solution scattering. Science Advances. 6(12):eaaz0981, (2020). 

Google scholar - the complete publication list 


The research is financed by the Swedish Research Council, EU, Kempe foundations and eSSENCE.

Head of research

Magnus Andersson
Associate professor


Participating departments and units at Umeå University

Department of Chemistry, Umeå Centre for Microbial Research (UCMR)

Research area

Chemical sciences, Infection biology

External funding

Swedish Research Council, The Kempe Foundation

External funding

Teaching assistants help in education

The Faculty of Science and Technology employs teaching assistants at more departments than before.

Latest update: 2023-10-17