Our research

DNA integrity is constantly threatened by radiation, chemicals and our own metabolism. Cells have developed clever ways to find and repair DNA damage, but these mechanisms can fail, causing premature ageing, neurodegenerative diseases, and cancer.

Considerable progress has been made to identify the factors involved in DNA repair. However, the intricacy of these protein complexes and the arrangement of our genome into a dynamic three-dimensional structure, chromatin, hinder a full understanding of these processes.

“It is very easy to answer many of these fundamental biological questions; you just look at the thing!”

(Richard Feynman)

We aim to uncover the precise mechanisms by which this molecular machinery operates. This involves identifying the specific proteins involved, elucidating their structures, and understanding how they work together to maintain genomic integrity.

Our lab combines biochemistry, structural biology, single-molecule imaging, biophysics, and functional studies to understand the composition, architecture and dynamics of DNA repair complexes in the context of chromatin.

Our goal is to provide mechanistic insights into the dynamic response to DNA damage to inform future prevention strategies and therapeutic approaches.

“All approaches at a higher level are suspect until confirmed at the molecular level.”

(Francis Crick)

In vitro reconstitution

We use biochemical reconstitution of recombinant macromolecular complexes in vitro.

This provides us with a tractable system to investigate their structure and function.

Our lab is fully equipped for protein over-expression and purification to obtain our samples.

CryoEM

We employ electron cryo-microscopy (cryoEM) to determine high resolution structures of DNA repair complexes.

Source: MRC Laboratory of Molecular Biology

Our department houses the Aarhus node of the Danish National CryoEM Facility (EMBION), providing access to excellent equipment for sample preparation, data collection and processing.

Single-molecule imaging

To add a temporal dimension to our understanding of these molecular processes, we use single-molecule imaging. This enables us to directly visualise the dynamic interactions of DNA repair complexes with chromatin in real time.

Direct visualization of FANCD2-FANCI on DNA (Alcón et al., 2024)

For this, we have access to the amazing expertise and instrumentation from our colleagues from ASiMoF at iNANO.

Biophysics

We use a range of techniques to measure molecular interactions.

Among our core facilities, we enjoy direct access to the fully equipped

Biophysics and Biochemistry Facility at MBG.

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