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ARC LIEF grant success: Bio21 Institute funded for cryo-EM and single crystal X-ray diffractometer
Establishment of a collaborative network, led by the University of Melbourne’s Bio21 Institute and Monash University to develop world leading capability in cryo-electron microscopy and protein structural biology
1 November 2016
A consortium of some of Australia's lead protein structural biologists, led by Professors Michael Parker and James Whisstock received $850,000 from the Australian Research Council to support the purchase of two new high resolution cryo-electron microscopes (cryo-EM) which will be located at the University of Melbourne's Bio21 Institute in Parkville, and at the Monash Biomedicine Discovery Institute, Clayton.
These instruments will provide researchers from around Victoria and Australia and New Zealand with world-leading capability to determine the three dimensional structure of proteins at atomic resolution and greatly facilitate studies aimed at understanding human diseases, and developing new drugs or biotechnology applications. They will provide additional capability to the existing Titan KRIOS instrument at the Ramaciotti Centre for Structural Cryo-Electron Microscopy and shorten the time taken to determine the structure of new proteins.
Other partners in this consortium include St Vincent’s Institute of Medical Research; the Walter and Eliza Hall Institute of Medical Research; the Peter MacCallum Cancer Institute, La Trobe University, RMIT, MacFarlane Burnett Centre for Medical Research, the Victor Chang Cardiac Research Institute, The University of New South Wales, Cardiff University, UK, The University of Auckland and CSL Ltd.
“Proteins complexes are the molecules of life and an understanding of how they work can lead to new drugs, pesticides, herbicides and the development of biosensors and nanomachines. The aim of protein structural biologist is to determine the three-dimensional structure of proteins at the atomic level in order to understand how they function and interact with other proteins or small molecules. Since the majority of drugs interact with proteins, these atomic structures have proved to be invaluable for the discovery and development of new drugs, herbicides and pesticides,” explains Professor Michael Parker, Bio21 Institute and St Vincent’s Institute of Medical Research.
“The development of new detector technology has led to a revolution in the use of cryo-EM for structural biology over the last five years with many near atomic resolution structures of important proteins now being determined by cryo-EM. Such discoveries routinely appear in leading scientific journals such as Nature and Science. However, in order to determine such structures many hundreds of experiments are typically required to optimize the preparation of a single protein to the point that it is likely to yield a detailed structure. The new microscopes include automation that will help overcome this major bottleneck,” explains Professor Whisstock, Director, ARC Centre of Excellence in Advanced Molecular Imaging, Scientific Head, EMBL Australia.
“Cryo-EM is revolutionizing our capacity to visualize large protein complexes and proteins that are embedded in cell walls, so-called membrane proteins, that are difficult to study by other approaches” says Professor Michael Parker.
“Examples of projects ready to benefit from the new equipment include: understanding how bacterial protein toxins punch holes in cell walls which may lead to the development of new biosensors, visualisation of drugs bound to an essential protein complex in the malarial parasite and the development of new antibiotics,” Professor Parker explains.
The establishment of advanced cryo-EM capability at the University of Melbourne's Bio21 Institute will greatly enhance existing expertise and capability in complementary approaches for determining protein structure" says the Professor Malcolm McConville, Bio21 Institute Director. The Institute already has one of the largest centres for nuclear magnetic resonance spectroscopy in the country which can be used to measure protein dynamics and changes in structure in solution.
Bio21 Institute researcher, Professor Jonathan White and colleagues from Monash and La Trobe Universities were also awarded $830,000 funding in the latest ARC LIEF round for an X-ray diffractometer instrument. Single crystal X-ray diffraction is an extremely powerful technique for elucidating the 3D structure of molecules from proteins to small molecules to new materials,” explains Professor White.
The co-location of cryo-EM, nuclear magnetic resonance spectrometry and single crystal X-ray diffractometry in the Parkville biomedical and science strips makes the Bio21 Institute one of the leading centres for protein structural biology in Australia and will cater for a large number of researchers from research institutes and hospitals in the precinct and beyond.
"These initiatives reflect a high level of collaboration and co-investment across multiple Universities and Medical Research Institutes which will greatly add to the capacity of Australian researchers to contribute to new discoveries and biotechnology applications in the biomedical and life sciences" says Professor Julie Willis, Acting Deputy Vice Chancellor for Research at the University of Melbourne.
Professor Malcolm McConville
Bio21 Molecular Science and Biotechnology Institute (Bio21 Institute)
T +613 83442342
Professor Michael W. Parker DPhil (Oxon) FAA FAHMS
ACRF Rational Drug Discovery Centre
St. Vincent's Institute of Medical Research
T: 03 9231 2499
M: 0400 150732.
E: mparker [at] svi.edu.au
Professor James Whisstock
Director, ARC Centre of Excellence in Advanced Molecular Imaging
Monash University, Clayton
M: 0418 170 585