IUCr 2023 Local Organising Committee
A Letter of Invitation
On behalf of the Local Organising Committee of the 26th Congress and General Assembly of the International Union of Crystallography and the Society of Crystallographers in Australia and New Zealand, we would like to extend our warmest invitation to you and your family to join us at the IUCr Congress in Melbourne, Australia from 22-29 August 2023.
Michael Parker
Helen Maynard-Casely
Daniel Eriksson
Megan Maher
Tom Peat
Melissa Call
Brendan Kennedy
Emily J Parker
David Aragão
Stuart Batten
Charlie Bond
Jack Clegg
Michael Parker
Michael Parker is Director of the Bio21 Institute, University of Melbourne and Head of Structural Biology, St. Vincent’s Institute of Medical Research in Melbourne. Michael completed a Bachelor Science degree with a major in chemistry at the Australian National University followed by a D. Phil. in protein crystallography from Oxford University and a postdoc at EMBL in Heidelberg, Germany. Michael returned to Australia to re-establish a protein crystallography laboratory at St. Vincent’s in 1991. Michael’s international reputation in protein crystallography derives from his research on the structures of membrane-associated proteins, especially pore-forming toxins and cytokine receptors, and of detoxifying enzymes. He has published over 300 papers and his work has been recognised with numerous awards including the 2011 Lemberg Medal of the Australian Society for Biochemistry and Molecular Biology, the 2011 Ramaciotti Medal for Excellence in Biomedical Research, and the 2012 Federation of Asian and Oceanian Biochemists and Molecular Biologists Award for Research Excellence. He was elected a Fellow of the Australian Academy of Science in 2010 and a Fellow of the Australian Academy of Health and Medical Sciences in 2015.
Helen Maynard-Casely
Helen Maynard-Casely (@Helen_E_MC) is a Senior Instrument Scientist at the Australian Centre for Neutron Scattering, ANSTO, and her research interest centre about the structures of materials relevant to the dwarf planets of our solar system. Her journey to exploring these icy worlds began with her degree in Planetary Sciences from University College London, and was followed by her PhD in high-pressure physics undertaken at the University of Edinburgh. Moving to Australia first to a post-doctoral position at the Australian Synchrotron, she moved to the Australian Centre for Neutron Scattering in 2013 to work on the High Intensity Diffractometer (known as Wombat). When not working on Wombat, Helen also enjoys promoting crystallography and science to as wide an audience as possible, for example she coordinated the 2014 Crystallography365 project (https://www.iycr2014.org/learn/crystallography365), was the 2019 Australian Institute of Physics ‘Women in Physics’ Lecturer and published her first children’s book (I heart Pluto) in 2020.
Daniel Eriksson
Daniel Eriksson received his PhD from Uppsala University, Sweden, in 2009, in the field of macromolecular X-ray crystallography. Following this, he worked as a Postdoctoral Research fellow with Bostjan Kobe, University of Queensland, on the bacterial, viral, and fungal pathogenesis of humans and plants. In 2014, Daniel joined the Australian Synchrotron, a landmark research infrastructure facility operated by ANSTO, as a beamline scientist in the macromolecular crystallography beamline team. He is an honorary lecturer with the Australian National University, where he has a long-standing collaboration with the Williams group in plant structural immunology. Daniel is currently in the project team for the next generation MX3 beamline, scheduled to start its user program in mid 2023.
Megan Maher
Megan Maher was awarded a PhD in Inorganic Chemistry from the University of Melbourne in 1998. She carried out postdoctoral research at the University of Sydney from 1998-2005, funded by a series of independent Fellowships. Between 2006-2007, she held the position of Team Leader in the Membrane Protein Crystallography Laboratory, headed by Professor So Iwata at Imperial College, London. In 2008 Megan returned to the Centenary Institute in Sydney, on a Career Development Fellowship funded by the Cancer Institute of NSW. Megan relocated to La Trobe University at the beginning of 2012 to take up a position as LIMS Senior Research Fellow. In 2015 she was appointed to the position of Senior Lecturer and Associate Professor in 2018. In 2017 Megan was awarded the Georgina Sweet Award for Women in Quantitative Biomedical Science and in 2018 an ARC Future Fellowship. Megan joined the School of Chemistry and Bio21 at the University of Melbourne in 2019 as part of the University’s Driving Research Momentum (DRM) strategy. Megan’s current research focuses on investigating the role of trace metals in biological systems, with a particular focus on the structural biology of metalloproteinase and integral membrane protein transporters.
Tom Peat
Tom Peat is a Senior Principal Research Scientist at CSIRO and an adjunct professor at UNSW. He received his BA from UC Berkeley (Biophysics and Biochemistry) and PhD from Columbia University, New York City (Molecular and Cellular Biophysics). Tom’s focus has been in protein structure determination by X-ray crystallography, as well as protein-protein and protein-substrate/inhibitor interactions. He has led or been involved in several fragment-based drug design and structure-based drug design campaigns and two of these are now in phase 1 clinical trials. His work has been performed both in government laboratories (Los Alamos National Lab and CSIRO) and in industry (Structural Genomix, OpenEye Scientific Software). Tom has collaborated widely, working with academics, industry and has deposited over 300 structures to the Protein Data Bank. He is a founder of two biotech companies in Melbourne: MecRX and Vittail. Both companies are developing inhibitors to cancer targets.
Melissa Call
Dr Melissa Call is a Laboratory Head in the Structural Biology Division at the Walter and Eliza Hall Institute. The Call laboratory studies the structural basis of signalling through cell-surface receptors that control key functions in immunity and haematopoiesis. The membrane-embedded domains of many receptors have features that guide receptor assembly in the endoplasmic reticulum and propagate signals through the membrane. However, it is extremely challenging to get structural data for these regions and as a consequence, our understanding of these processes is limited. Through the crystallisation of the Glycophorin A transmembrane domain, we have shown that the transmembrane domains of even single-spanning receptor subunits are amenable to crystallographic techniques and have validated that native structures can be obtained. Furthermore, we have crystallised the DAP12 transmembrane domain, which has yielded insights in the mechanistic basis of NK cell receptor assembly. We are applying these techniques to better understand how type I cytokine receptors mechanically communicate ligand-binding events across the lipid bilayer and how the unique physical and chemical characteristics of the membrane environment contribute to and regulate receptor function. Dr Melissa Call received her PhD in Molecular Medicine from the University of Auckland was a Postdoctoral Fellow at the Dana-Farber Cancer Institute in Boston where she studied the mechanisms of peptide-exchange in the MHC class II peptide-presentation pathway. She joined the Structural Biology Division at the Walter and Eliza Hall Institute in 2010 and runs a joint research programme with Dr Matthew Call.
Brendan Kennedy
Professor Brendan Kennedy is a Professor of Chemistry at the University of Sydney, where his major research interests are in structure-property relationships in metal oxides, with a particular interest in structural and magnetic phase transitions. He received his PhD in inorganic chemistry from Monash University and following post-doctoral positions at Oxford University and the Australian National University moved to the University of Sydney to establish a solid-state chemistry laboratory. His research makes extensive use of synchrotron and neutron powder diffraction and spectroscopy. He has published over 350 papers and his work has been recognised with numerous awards, including an Australian Institute of Nuclear Science and Engineering Gold Medal. He was chair of the 2005 International Conference on Neutron Scattering held in Sydney and is a member of the local organising committee for the XAFS International Conference on X-Ray Absorption Fine Structure 2021 and 2022.
He is a past president of the Society of crystallographers in Australia and New Zealand and of the Australian Neutron Beam Users group. He is currently a Member of the IUCr Commission for Powder Diffraction and President of the Asia-Oceania Neutron Scattering Association.
David Aragão
David Aragão studied organic chemistry at the Universidade Nova de Lisboa (FCT-UNL, Portugal, 1994-2001). From early undergraduate days he got interested in structural biology having spent time in international laboratories like the EMBL, Grenoble, France (1999) and University of Georgia, Athens, USA (2000). After graduating in chemistry David worked for a 2-year period as a research assistant in Protein Crystallography with particular emphasis on metalloproteins (2000-2001). From here he then followed to a joined Ph.D between the European Synchrotron Radiation Facility (ESRF, France) and the Instituto de Tecnologia Química e Biológica (ITQB-UNL, Portugal) – 2002 to 2007 – where the metalloproteins research path was expanded to enzymes involved in bacterial biofilm formation. In 2008 he moved to Ireland, under Prof. Martin Caffrey’s supervision, as a NHI funded Postdoctoral Research Fellow (University of Limerick) and later successfully obtaining a prestigious IEF Marie Curie Fellowship to work at Trinity College Dublin. During this period he specialized in the membrane protein field working in diverse important targets from GPCRs, membrane metalloproteins and several P. aeruginosa membrane proteins involved in biofilm, membrane kinetics, ABC-transporters and others. In 2011 he joined the Australian Synchrotron for a two year period as a beamline postdoc and after a brief stunt jointly appointed by the Australian Synchrotron and Victor Chang Cardiac Research Institute he became a Beamline Scientist at the Australian Synchrotron. Later he moved to the United Kingdom where he currently has the role of Senior Beamline Scientist at the I04 Diamond Light Source beamline. His current research interests lie in field of membrane structural biology namely viral capsids, nuclear import, membrane metalloproteins, ABC- transporters, ATP synthases but also crystallography and beamline method developments from hardware to software developments related to micron-beams, lipid cubic phase, multi-crystal data merging just to name a few.
Stuart Batten
Stuart Batten completed his PhD (1996) at the University of Melbourne with Richard Robson and Bernard Hoskins. This was followed by postdoctoral positions at Bristol, Melbourne and Monash, including two Australian Research Council Fellowships. He commenced a Lectureship at Monash in 2006, and has been a full Professor there since 2012. His research, detailed in more than 300 publications, is mainly in the areas of crystal engineering, coordination polymers, supramolecular chemistry, inorganic chemistry, and chemical crystallography. He is lead author of a book entitled Coordination Polymers: Design, Analysis and Application (RSC 2009; with DR Turner and SM Neville). His research has attracted over 26,000 citations (h-index = 84), leading to recognition as a Highly Cited Researcher (2014, 2015, 2016) and several other awards, including a Thomson Scientific Citation Award (2008), the Le Fèvre Memorial Prize (2008), and the Rennie Memorial Medal (2002). He is also a former President of the Society of Crystallographers in Australia and New Zealand (SCANZ), former Chair of the IUCr Commission on Structural Chemistry, and co-founder and co-chair of the inaugural Australasian Crystallography School.