When: 2 July, 2026, 13:00 - 14:30
Where: LINXS, workshop room on the 3rd floor (The Loop, Rydbergs torg 4, 224 84) or digitally via Zoom
Speaker: Marjolein Thunnissen, Life Science Advisor MAX IV, Lund University, Lund
Title: Illuminating Viruses: Synchrotron Methods in Virology
Abstract
When considering how synchrotrons contribute to virology research, structure determination of viral proteins and entire capsids is often the first application that comes to mind. However, synchrotron facilities provide a much broader range of techniques than classical crystallographic approaches alone, enabling researchers to investigate many additional aspects of viral biology. Advanced synchrotron-based methods can be used to study dynamic processes such as virus assembly, attachment to host cells, cellular entry and exit mechanisms, and virus-induced changes in tissue and organ pathology. These techniques also play an important role in vaccine development, antiviral drug discovery, and the characterization of host–pathogen interactions at multiple spatial and temporal scales. This lecture will present an overview of the synchrotron techniques available for virology research and highlight selected scientific examples that demonstrate their diverse applications and impact.
Biography
Marjolein Thunnissen, currently serving as senior science advisor at MAX IV, involved in coordinating activities towards the life sciences community. These encompass a wide spectrum of applications, including protein crystallography, small angle X-ray scattering, cutting-edge imaging techniques, X-ray absorption methods, and more. Marjolein plays a pivotal role in fostering relationships with users, both from academic and industrial backgrounds, while also spearheading educational and training initiatives. Marjolein's academic journey commenced at the University of Groningen, the Netherlands, where she embarked on her undergraduate and doctoral studies in chemistry. It was during her undergraduate years that her fascination with unraveling the intricate structure-function relationships of proteins through X-ray diffraction was ignited. Her main scientific interests have been inflammation and infection. She has solved several protein structures, amongst which the structure of Leukotriene A4 Hydrolase, the first member of the M1 group of zinc metalloproteases for which a structure got determined.
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