Melbourne, Australia
Melbourne, Australia

The Australian Synchrotron is a 3 GeV synchrotron radiation facility built in Melbourne, Victoria and opened on 31 July 2007.The circular building was designed by Architectus in conjunction with Thiess, while the lattice design was performed substantially by Professor John Boldeman. The Synchrotron building is located in Clayton near the Monash University Clayton Campus.The Australian Synchrotron is a light source facility . It uses particle accelerators to produce a beam of high energy electrons which are placed within a storage ring that circulates the electrons to create synchrotron light. The light is directed down separate beamlines at the end of which may be placed a variety of experimental equipment contained within the endstations. Wikipedia.


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News Article | September 14, 2016
Site: www.nanotech-now.com

Abstract: The discovery, led by Associate Professor Brian Abbey at La Trobe in collaboration with Associate Professor Harry Quiney at the University of Melbourne, has been published in the journal Science Advances. Their findings reverse what has been accepted thinking in crystallography for more than 100 years. The team exposed a sample of crystals, known as Buckminsterfullerene or Buckyballs, to intense light emitted from the world's first hard X-ray free electron laser (XFEL), based at Stanford University in the United States. The molecules have a spherical shape forming a pattern that resembles panels on a soccer ball. Light from the XFEL is around one billion times brighter than light generated by any other X-ray equipment --even light from the Australian Synchrotron pales in comparison. Because other X-ray sources deliver their energy much slower than the XFEL, all previous observations had found that the X-rays randomly melt or destroy the crystal. Scientists had previously assumed that XFELs would do the same. The result from the XFEL experiments on Buckyballs, however, was not at all what scientists expected. When the XFEL intensity was cranked up past a critical point, the electrons in the Buckyballs spontaneously re-arranged their positions, changing the shape of the molecules completely. Every molecule in the crystal changed from being shaped like a soccer ball to being shaped like an AFL ball at the same time. This effect produces completely different images at the detector. It also altered the sample's optical and physical properties. "It was like smashing a walnut with a sledgehammer and instead of destroying it and shattering it into a million pieces, we instead created a different shape - an almond!" Assoc. Prof. Abbey said. "We were stunned, this is the first time in the world that X-ray light has effectively created a new type of crystal phase" said Associate Professor Quiney, from the School of Physics, University of Melbourne. "Though it only remains stable for a tiny fraction of a second, we observed that the sample's physical, optical and chemical characteristics changed dramatically, from its original form," he said. "This change means that when we use XFELs for crystallography experiments we will have to change the way interpret the data. The results give the 100-year-old science of crystallography a new, exciting direction," Assoc. Prof. Abbey said. "Currently, crystallography is the tool used by biologists and immunologists to probe the inner workings of proteins and molecules -- the machines of life. Being able to see these structures in new ways will help us to understand interactions in the human body and may open new avenues for drug development." ### The study was conducted by researchers from the ARC Centre of Excellence in Advanced Molecular Imaging, La Trobe University, the University of Melbourne, Imperial College London, the CSIRO, the Australian Synchrotron, Swinburne Institute of Technology, the University of Oxford, Brookhaven National Laboratory, the Stanford Linear Accelerator (SLAC), the BioXFEL Science and Technology Centre, Uppsala University and the Florey Institute of Neuroscience and Mental Health. For more information, please click If you have a comment, please us. Issuers of news releases, not 7th Wave, Inc. or Nanotechnology Now, are solely responsible for the accuracy of the content.


News Article | December 7, 2016
Site: www.eurekalert.org

Every 18 seconds someone dies from tuberculosis (TB). It is the world's most deadly infectious disease. Mycobacterium tuberculosis, the causative agent of TB, has infected over one-third of the entire human population with an annual death toll of approximately 1.5 million people. For the first time, an international team of scientists from Monash and Harvard Universities have seen how, at a molecular level, the human immune system recognises TB infected cells and initiates an immune response. Their findings, published in Nature Communications, are the first step toward developing new diagnostic tools and novel immunotherapies. Lead author, Professor Jamie Rossjohn says one of the main reasons for our current lack of knowledge comes down to the complexity of the bacterium itself. Working with Professor Branch Moody's team at Harvard, they have begun to gain key insight into how the immune system can recognise this bacterium. Crucial to the success of M. tuberculosis as a pathogen is its highly unusual cell wall that not only serves as a barrier against therapeutic attack, but also modulates the host immune system. Conversely, its cell wall may also be the "Achilles' heel" of mycobacteria as it is essential for the growth and survival of these organisms. This unique cell wall is comprised of multiple layers that form a rich waxy barrier, and many of these lipid -- also known as fatty acids -- components represent potential targets for T-cell surveillance. Specifically, using the Australian Synchrotron, the team of scientists have shown how the immune system recognises components of the waxy barrier from the M. tuberculosis cell wall. "With so many people dying from TB every year, any improvements in diagnosis, therapeutic design and vaccination will have major impacts," Professor Moody says. "Our research is focussed on gaining a basic mechanistic understanding of an important biomedical question. And may ultimately provide a platform for designing novel therapeutics for TB and treat this devastating disease," Professor Rossjohn concludes. Professor Jamie Rossjohn is a Chief Investigator on the Australian Research Council Centre of Excellence in Advanced Molecular Imaging. The $39 million ARC-funded Imaging CoE develops and uses innovative imaging technologies to visualise the molecular interactions that underpin the immune system. Featuring an internationally renowned team of lead scientists across five major Australian Universities and academic and commercial partners globally, the Centre uses a truly multi scale and programmatic approach to imaging to deliver maximum impact. The Imaging CoE is headquartered at Monash University with four collaborating organisations - La Trobe University, the University of Melbourne, University of New South Wales and the University of Queensland. Professor Rossjohn is also a researcher at the Monash Biomedicine Discovery Institute. Committed to making the discoveries that will relieve the future burden of disease, the newly established Monash Biomedicine Discovery Institute at Monash University brings together more than 120 internationally-renowned research teams. Our researchers are supported by world-class technology and infrastructure, and partner with industry, clinicians and researchers internationally to enhance lives through discovery.


Schuettfort T.,University of Cambridge | Thomsen L.,Australian Synchrotron | McNeill C.R.,Monash University
Journal of the American Chemical Society | Year: 2013

The molecular orientation and microstructure of films of the high-mobility semiconducting polymer poly(N,N-bis-2-octyldodecylnaphthalene-1,4,5,8-bis- dicarboximide-2,6-diyl-alt-5,5-2,2-bithiophene) (P(NDI2OD-T2)) are probed using a combination of grazing-incidence wide-angle X-ray scattering (GIWAXS) and near-edge X-ray absorption fine-structure (NEXAFS) spectroscopy. In particular a novel approach is used whereby the bulk molecular orientation and surface molecular orientation are simultaneously measured on the same sample using NEXAFS spectroscopy in an angle-resolved transmission experiment. Furthermore, the acquisition of bulk-sensitive NEXAFS data enables a direct comparison of the information provided by GIWAXS and NEXAFS. By comparison of the bulk-sensitive and surface-sensitive NEXAFS data, a distinctly different molecular orientation is observed at the surface of the film compared to the bulk. While a more "face-on" orientation of the conjugated backbone is observed in the bulk of the film, consistent with the lamella orientation observed by GIWAXS, a more "edge-on" orientation is observed at the surface of the film with surface-sensitive NEXAFS spectroscopy. This distinct edge-on surface orientation explains the high in-plane mobility that is achieved in top-gate P(NDI2OD-T2) field-effect transistors (FETs), while the bulk face-on texture explains the high out-of-plane mobilities that are observed in time-of-flight and diode measurements. These results also stress that GIWAXS lacks the surface sensitivity required to probe the microstructure of the accumulation layer that supports charge transport in organic FETs and hence may not necessarily be appropriate for correlating film microstructure and FET charge transport. © 2012 American Chemical Society.


News Article
Site: www.asminternational.org

The University of New South Wales and Monash University, Australia, announce that a team of researchers has developed a high-strength magnesium-lithium alloy with density of 1.4 g/cm3, 50% less than aluminum and 30% less than magnesium. The researchers have shown that the alloy forms a protective layer of carbonate-rich film upon exposure to air, making it immune to corrosion. The finding is published online in the 19 October edition of Nature Materials. Prof.  Michael Ferry, of UNSW's School of Materials Science and Engineering, says that the excellent corrosion resistance of the alloy was observed by chance, when the team noticed that a heat-treated sample in a beaker of salt water showed no corrosion after several hours. Normally magnesium would have been extensively corroded. The researchers then designed a magnesium-lithium alloy of specific composition together with a processing sequence consisting of hot extrusion, heating and water quenching, low-temperature aging, and cold rolling. "This is the first magnesium-lithium alloy to stop corrosion from irreversibly eating into the alloy, as the balance of elements interacts with ambient air to form a surface layer which, even if scraped off repeatedly, rapidly reforms to create reliable and durable protection," says Prof.  Ferry. The UNSW team partnered with scientists on the Powder Diffraction beamline at the Australian Synchrotron, to confirm that the alloy contains a unique nanostructure that enables the formation of a protective surface film. Prof. Nick Birbilis (shown in the photo), School of Materials Science and Engineering at Monash University, says viewing unprecedented structural detail of the alloy through the Australian Synchrotron will enable the team  to work toward commercializing the new metal. ‘We're aiming to take the knowledge gleaned at the Australian Synchrotron to incorporate new techniques into the mass-production of this unique alloy in sheets of varying thickness, in a standard processing plant," Prof. Birbilis said.


News Article | September 12, 2016
Site: www.rdmag.com

New research has found that venom extracted from a species of marine cone snail could hold the key to developing 'ultra-fast-acting' insulins, leading to more efficient therapies for diabetes management. Researchers from Australia and the US have successfully determined the three-dimensional structure of a cone snail venom insulin, revealing how these highly efficient natural proteins called Con-Ins G1 can operate faster than human insulin. The teams also discovered that Con-Ins G1 was able bind to human insulin receptors, signifying the potential for its translation into a human therapeutic. Associate Professor Mike Lawrence from Melbourne's Walter and Eliza Hall Institute of Medical Research led a collaborative study between the University of Utah, the Monash Institute of Pharmaceutical Sciences, La Trobe University and Flinders University in Australia. Associate Professor Lawrence, a specialist in the structure of insulins and their receptors, said the teams utilised the Australian Synchrotron to create and analyse the three-dimensional structure of this cone snail venom insulin protein with exciting results. "We found that cone snail venom insulins work faster than human insulins by avoiding the structural changes that human insulins undergo in order to function -- they are essentially primed and ready to bind to their receptors, " Associate Professor Lawrence said. Associate Professor Lawrence said human insulins could be considered 'clunky' by comparison. "The structure of human insulins contain an extra 'hinge' component that has to open before any 'molecular handshake' or connection between insulin and receptor can take place. "By studying the three-dimensional structure of this snail venom insulin we've found how to dispense with this 'hinge' entirely, which may accelerate the cell signalling process and thus the speed with which the insulin takes effect." Associate Professor Lawrence said. Published today in Nature Structural and Molecular Biology, the team's findings build on earlier studies from 2015, when the University of Utah reported that the marine cone snail Conus geographus used an insulin-based venom to trap its prey. Unsuspecting fish prey would swim into the invisible trap and immediately become immobilised in a state of hyperglycaemic shock induced by the venom. Dr Helena Safavi-Hemami from the University of Utah said it was fascinating to uncover how the cone snail insulin was able to have such a rapid effect on its prey and, furthermore, that the peptide had therapeutic potential in humans. "We were thrilled to find that the principles of cone snail venom insulins could be applied to a human setting," Dr Safavi-Hemami said. "Our Flinders University colleagues have shown that the cone snail insulin can 'switch on' human insulin cell signalling pathways, meaning the cone snail insulin is able to successfully bind to human receptors," Dr Safavi-Hemami said. "The next step in our research, which is already underway, is to apply these findings to the design of new and better treatments for diabetes, giving patients access to faster-acting insulins," she said.


News Article | September 13, 2016
Site: www.chromatographytechniques.com

New research has found that venom extracted from a species of marine cone snail could hold the key to developing "ultra-fast-acting" insulins, leading to more efficient therapies for diabetes management. Researchers from Australia and the U.S. have successfully determined the three-dimensional structure of a cone snail venom insulin, revealing how these highly efficient natural proteins called Con-Ins G1 can operate faster than human insulin. The teams also discovered that Con-Ins G1 was able bind to human insulin receptors, signifying the potential for its translation into a human therapeutic. Associate Professor Mike Lawrence from Melbourne's Walter and Eliza Hall Institute of Medical Research led a collaborative study between the University of Utah, the Monash Institute of Pharmaceutical Sciences, La Trobe University and Flinders University in Australia. Lawrence, a specialist in the structure of insulins and their receptors, said the teams utilized the Australian Synchrotron to create and analyze the three-dimensional structure of this cone snail venom insulin protein with exciting results. "We found that cone snail venom insulins work faster than human insulins by avoiding the structural changes that human insulins undergo in order to function -- they are essentially primed and ready to bind to their receptors, " Lawrence said. He said human insulins could be considered "clunky" by comparison. "The structure of human insulins contain an extra 'hinge' component that has to open before any 'molecular handshake' or connection between insulin and receptor can take place. By studying the three-dimensional structure of this snail venom insulin we've found how to dispense with this 'hinge' entirely, which may accelerate the cell signalling process and thus the speed with which the insulin takes effect." Published in Nature Structural and Molecular Biology, the team's findings build on earlier studies from 2015, when the University of Utah reported that the marine cone snail Conus geographus used an insulin-based venom to trap its prey. Unsuspecting fish prey would swim into the invisible trap and immediately become immobilised in a state of hypoglycaemic shock induced by the venom. Helena Safavi-Hemami from the University of Utah said it was fascinating to uncover how the cone snail insulin was able to have such a rapid effect on its prey and, furthermore, that the peptide had therapeutic potential in humans. "We were thrilled to find that the principles of cone snail venom insulins could be applied to a human setting. Our Flinders University colleagues have shown that the cone snail insulin can 'switch on' human insulin cell signalling pathways, meaning the cone snail insulin is able to successfully bind to human receptors. The next step in our research, which is already underway, is to apply these findings to the design of new and better treatments for diabetes, giving patients access to faster-acting insulins," she said.


News Article | February 27, 2017
Site: www.eurekalert.org

New light on a key factor involved in diseases such as Parkinson's disease, gastric cancer and melanoma has been cast through latest University of Otago, New Zealand, research carried out in collaboration with Australian scientists. In new findings published in leading international journal PNAS, the team of researchers, led by Otago Department of Biochemistry's Dr Peter Mace, studied a protein called Apoptosis signal-regulating kinase 1 (ASK1). Along with other kinases, ASK1 acts as a signalling protein that controls many aspects of cellular behaviour. Kinases put tags onto other proteins that can turn them on, off, which in turn can make a cell divide, die, move or any number of other responses. Dr Mace says ASK1 plays an important role in controlling how a cell responds to cell damage, and can push the cell towards a process of programmed cell death for the good of the body, if damage to a cell is too great. This key role is reflected in ASK1's name - apoptosis is an Ancient Greek word meaning "falling off" - and is used to describe the process of programmed dying of cells, rather than their loss by injury. The research team determined ASK1's molecular structure through crystallography studies and also performed biochemical experiments to better understand the protein. They found that ASK1 has unexpected parts to its structure that help control how the protein is turned on, and that an entire family of ASK kinases share these features. "We now know a lot more about how ASK1 gets turned on and off - this is important because in diseases such as Parkinson's, stomach cancer and melanoma, there can be either too much or too little ASK1 activity". Dr Mace says that the new findings add to our understanding of how cells can trigger specific responses to different threats or damage encountered. Such threats can include oxidants, which damage the body's tissues by causing inflammation. He adds that kinases are excellent targets for developing new drugs because they have a "pocket" in their structure that such compounds can bind to, but to develop better drugs we need to understand far more about how they are controlled. This is the goal of several projects in his lab, he says. The study is a collaboration between Otago researchers and scientists at the Walter and Eliza Hall Institute (WEHI) in Melbourne, and at the Australian Synchrotron. Otago alumnus Tom Caradoc-Davies, who works at the MX Beamline, collected data that was critical to the project. Synchrotron access was enabled by the New Zealand Synchrotron Group, which is coordinated by the Royal Society of New Zealand and supported by all New Zealand universities in partnership with the Government. The synchrotron is crucial to many other research projects from Otago and throughout New Zealand.


News Article | February 27, 2017
Site: phys.org

In new findings published in leading international journal PNAS, the team of researchers, led by Otago Department of Biochemistry's Dr Peter Mace, studied a protein called Apoptosis signal-regulating kinase 1 (ASK1). Along with other kinases, ASK1 acts as a signalling protein that controls many aspects of cellular behaviour. Kinases put tags onto other proteins that can turn them on, off, which in turn can make a cell divide, die, move or any number of other responses. Dr Mace says ASK1 plays an important role in controlling how a cell responds to cell damage, and can push the cell towards a process of programmed cell death for the good of the body, if damage to a cell is too great. This key role is reflected in ASK1's name - apoptosis is an Ancient Greek word meaning "falling off" - and is used to describe the process of programmed dying of cells, rather than their loss by injury. The research team determined ASK1's molecular structure through crystallography studies and also performed biochemical experiments to better understand the protein. They found that ASK1 has unexpected parts to its structure that help control how the protein is turned on, and that an entire family of ASK kinases share these features. "We now know a lot more about how ASK1 gets turned on and off - this is important because in diseases such as Parkinson's, stomach cancer and melanoma, there can be either too much or too little ASK1 activity". Dr Mace says that the new findings add to our understanding of how cells can trigger specific responses to different threats or damage encountered. Such threats can include oxidants, which damage the body's tissues by causing inflammation. He adds that kinases are excellent targets for developing new drugs because they have a "pocket" in their structure that such compounds can bind to, but to develop better drugs we need to understand far more about how they are controlled. This is the goal of several projects in his lab, he says. The study is a collaboration between Otago researchers and scientists at the Walter and Eliza Hall Institute (WEHI) in Melbourne, and at the Australian Synchrotron. Otago alumnus Tom Caradoc-Davies, who works at the MX Beamline, collected data that was critical to the project. Synchrotron access was enabled by the New Zealand Synchrotron Group, which is coordinated by the Royal Society of New Zealand and supported by all New Zealand universities in partnership with the Government. The synchrotron is crucial to many other research projects from Otago and throughout New Zealand. More information: Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1, PNAS, www.pnas.org/cgi/doi/10.1073/pnas.1620813114


Chromium supplements are widely consumed for their antidiabetic activity as chromium(III) enhances the insulin sensitivity of cells. In particular, orthomolecular practitioners believe in the beneficial effects of providing the body with extra amounts of essential trace elements. As Australian and American scientists now report in the journal Angewandte Chemie, chromium(III) dietary supplements are oxidized to a certain extent in living cells to their carcinogenic and genotoxic chromium(V) and chromium(VI) counterparts, which raises questions about potential risks of such therapies. In the body, chromium(III) is known to be able to enhance the effects of insulin and oral antidiabetic drugs. Thus it has been proposed that the daily intake of a certain amount of chromium lowers the blood glucose level. However, in higher oxidation states, chromium compounds can have detrimental effects on DNA and thus can cause cancer. There is growing concern about possible oxidation pathways during the metabolic transformation of the chromium(III)-containing drugs in the cell. With the aim at getting more insight into the fate of the chromium compounds after their intake, Peter A. Lay from the University of Sydney, Australia, and his colleagues employed X-ray fluorescence microscopy (XFM) elemental mapping and microfocus X-ray absorption near-edge structure (µ-XANES) analysis on single chromium(III)-treated adipocytes, making use of the Australian Synchrotron facility and of resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility. By carrying out XFM analysis, Lay and his colleagues found that the chromium was confined in "hotspots", and the µ-XANES data revealed that these hotspots did not only contain chromium(III). The authors conclude: "This finding unambiguously confirmed the presence of high oxidation states of chromium." After having established the presence of higher oxidation states, the scientists also modelled the possible chromium compounds and identified chromium(V) and chromium(VI) compounds. The question remained why the chromium was oxidized in the overall reducing environment of the cells. The authors present a possible and plausible explanation: During cell signaling, and especially insulin signaling, strong oxidants such as hydrogen peroxide are formed, which will trigger the formation of reactive chromium(V) and chromium(VI) intermediates. "This raises concern over the possible carcinogenicity of chromium(III) compounds and the risks of long-term chromium(III) nutritional supplementation," the authors say. Although concerns have been raised for some time about the efficacy and safety of such supplements, many authorities and a large community of orthomolecular practitioners still recommend such treatments. Thus Lay and his colleagues urge for future studies: "In light of these findings, there is a need for epidemiological studies to ascertain whether chromium(III) supplements alter cancer risk." Explore further: Study: Water chemical can cause cancer More information: Lindsay E. Wu et al. Carcinogenic Chromium(VI) Compounds Formed by Intracellular Oxidation of Chromium(III) Dietary Supplements by Adipocytes, Angewandte Chemie International Edition (2015). DOI: 10.1002/anie.201509065


De Jonge M.D.,Australian Synchrotron | Vogt S.,Argonne National Laboratory
Current Opinion in Structural Biology | Year: 2010

Hard X-ray fluorescence microscopy is well-suited to in-situ investigations of trace metal distributions within whole, unstained, biological tissue, with sub-parts-per-million detection achievable in whole cells. The high penetration of X-rays indicates the use of X-ray fluorescence tomography for structural visualization, and recent measurements have realised sub-500-nm tomography on a 10-μm cell. Limitations of present approaches impact the duration of an experiment and imaging fidelity. Developments in X-ray resolution, detector speed, cryogenic environments, and the incorporation of auxiliary signals are being pursued within the synchrotron community. Several complementary approaches to X-ray fluorescence tomography will be routinely available to the biologist in the near future. We discuss these approaches and review applications of biological relevance. © 2010 Elsevier Ltd.

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