Dr Michael Landsberg

Biography

My undergraudate and Honours studies, majoring in Chemistry, were completed at Central Queensland University and the CSIRO (JM Rendel laboratories) before I moved to the University of Queensland to study a PhD in Biochemistry (awarded 2003). I then moved to a postdoctoral position at the Institute for Molecular Bioscience, securing promotion to Senior Research Officer in 2009 and spending time as a Visiting Scientist at Harvard Medical School (2008) and the Victor Chang Cardiac Research Institute (2010). I joined the School of Chemistry and Molecular Biosciences as a Senior Lecturer in 2016.

Research Interest

Research in my lab is motivated by the fundamental requirement to improve our understanding of the way in which large and intricately-assembled macromolecular machines come together and function. Since the arrival of the 'genomic era' at the start of the 21st century, science has benefited from an unprecedented capability to identify genes and proteins that are linked to health and human disease. But it has now become clear that a list of genes involved in disease is not enough for a number of reasons, but perhaps most importantly because genes and the proteins they encode rarely act in isolation. Rather, they form (often large) networks of interactions with proteins and other molecules. Obtaining a full appreciation of how proteins come together and interact, either transiently or more permanently, to achieve cellular function(s) is a core underlying theme of our labs research. We have a particular interest in understanding fundamental mechanisms that enable infection by viruses and contribute to virulence associated with pathogenic micro-organisms. To achieve this, study the molecular structure of the proteins and protein complexes involved, principally using cryo-electron microscopy (cryo-EM). Historically, cryo-EM has bridged the resolution gap between light microscopy (which can visualise small cells and large subcellular organelles) and high resolution methods for studying the structure of smaller proteins and some protein complexes (X-ray crystallography and biomolecular NMR). However, recent exciting developments in cryo-EM imaging have placed ourselves and other cryo-EM research labs around the world in a position where we can no directly visualise the large molecular machines (and even smaller assemblies) at levels of detail which rival the capabilities of protein crystallography and NMR.