Research

We apply a broad range of molecular biology, structural biology, and bio-imaging methods in our research. Cryogenic transmission electron microscopy (cryo-EM) is a versatile method for structural studies of small proteins, large complexes, viruses, and even organelles or sections of cells. Determining the detailed structures of different cellular components contributes to understanding of their basic functions and how these functions are impaired in disease.

Here you can find more about our current research projects. Please feel free to come and talk to us about potential collaborations. We are also constantly considering new members to join our growing team. 

Endogenous levels of protein expression are often too low for traditional structural methods. We focus on the development of methods that allow both endogenous tagging of target complexes as well as specific capture of tagged target proteins directly on cryo electron microscopy grids. These methods facilitate structure determination without overexpression and enable characterisation of rare and fragile complexes directly from native sources.

This project is funded by the Academy of Finland consortium grant (SEMMA) and is a collaboration with Aalto University. 

Membrane trafficking involves several processes mediating the transport of cargo within cellular vesicles. This transport can take place between different organelles including the endoplasmic reticulum (ER), the Golgi complex, endosomes, lysosomes, and autophagosomes in the same cell, or across the cell membrane to the adjacent cells. Our research aims at addressing key molecular mechanisms in vesicular transport by cryogenic electron microscopy (cryo-EM) to determine how cargo can be transported within different vesicles among different organelles, how the vesicles are formed and regulated, and how mutations affect these mechanisms.

The project (CellCargo) is funded by Jane and Aatos Erkko Foundation.

Computational cryo-EM methods are best suited for solving  structures of macromolecular complexes that have high-symmetry and regular structures. We develop new tools to address structures with inherent flexibility and mismatches in symmetry. Such structures include many key cellular components as well as viruses and virus–receptor and virus–antibody complexes. 

We are taking advantage of CRISPR genome editing to tag endogenous proteins and especially membrane proteins for purification and detection. We are applying (correlative) light microscopy and cryogenic electron microscopy (both single particle and and tomography) to decipher in situ structural organizations of these proteins on the plasma membrane and further to gain mechanistic insight into the underlying molecular mechanism of inter-cellular transport.

The project is funded by Sigrid Juselius Foundation.