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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.
Research projects are available in the areas of:
characterisation of bacterial ABC toxins
molecular mechanisms of Vps4-mediated viral infection
structure and function of molecular machines
development of methods for single particle cryo-EM.
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.
Research projects are available in the areas of:
characterisation of bacterial ABC toxins
molecular mechanisms of Vps4-mediated viral infection
structure and function of molecular machines
development of methods for single particle cryo-EM.
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Jason N Busby, Sarah Trevelyan,Cassandra L Pegg,Edward D Kerr,Benjamin L Schulz,Irene Chassagnon,Michael J Landsberg, Mitchell K Weston,Mark R H Hurst,J Shaun Lott
IUCrJ (2024)
Jason N. Busby, Sarah Trevelyan,Cassandra L. Pegg,Edward D. Kerr,Benjamin L. Schulz,Irene Chassagnon,Michael J. Landsberg, Mitchell K. Weston,Mark R. H. Hurst,J. Shaun Lott
IUCrJno. 3 (2024)
Ariel Isaacs,Yu Shang Low, Kyle L. Macauslane, Joy Seitanidou,Cassandra L. Pegg,Stacey T. M. Cheung,Benjamin Liang,Connor A. P. Scott,Michael J. Landsberg,Benjamin L. Schulz,Keith J. Chappell,Naphak Modhiran,
Nature Communicationsno. 1 (2023): 1-10
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Biochemical Society transactionsno. 3 (2023): 1235-1244
PROTEIN SCIENCE (2023)
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Applied Biosciencesno. 2 (2022): 163-178
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