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  • richardmitnick 2:45 pm on February 23, 2017 Permalink | Reply
    Tags: ANL APS, , Instrument finds new earthly purpose, , , , Spectrometry, ,   

    From Symmetry: “Instrument finds new earthly purpose” 

    Symmetry Mag

    Symmetry

    02/23/17
    Amanda Solliday

    1
    Nordlund and his colleagues—Sangjun Lee, a SLAC postdoctoral research fellow, and Jamie Titus, a Stanford University doctoral student (pictured above at SSRL, from left: Lee, Titus and Nordlund)—have already used the transition-edge-sensor spectrometer at SSRL to probe for nitrogen impurities in nanodiamonds and graphene, as well as closely examine the metal centers of proteins and bioenzymes, such as hemoglobin and photosystem II. The project at SLAC was developed with 
support by the Department of Energy’s Laboratory Directed Research and Development.
    Andy Freeberg, SLAC National Accelerator Laboratory

    Detectors long used to look at the cosmos are now part of X-ray experiments here on Earth.

    Modern cosmology experiments—such as the BICEP instruments and the in Antarctica—rely on superconducting photon detectors to capture signals from the early universe.

    BICEP 3 at the South Pole
    BICEP 3 at the South Pole

    Keck Array
    Keck Array at the South Pole

    These detectors, called transition edge sensors, are kept at temperatures near absolute zero, at only tenths of a Kelvin. At this temperature, the “transition” between superconducting and normal states, the sensors function like an extremely sensitive thermometer. They are able to detect heat from cosmic microwave background radiation, the glow emitted after the Big Bang, which is only slightly warmer at around 3 Kelvin.

    Scientists also have been experimenting with these same detectors to catch a different form of light, says Dan Swetz, a scientist at the National Institute of Standards and Technology. These sensors also happen to work quite well as extremely sensitive X-ray detectors.

    NIST scientists, including Swetz, design and build the thin, superconducting sensors and turn them into pixelated arrays smaller than a penny. They construct an entire X-ray spectrometer system around those arrays, including a cryocooler, a refrigerator that can keep the detectors near absolute zero temperatures.

    2

    TES array and cover shown with penny coin for scale.
    Dan Schmidt, NIST

    Over the past several years, these X-ray spectrometers built at the NIST Boulder MicroFabrication Facility have been installed at three synchrotrons at US Department of Energy national laboratories: the National Synchrotron Light Source at Brookhaven National Laboratory, the Advanced Photon Source [APS] at Argonne National Laboratory and most recently at the Stanford Synchrotron Radiation Lightsource [SSRL] at SLAC National Accelerator Laboratory.

    BNL NSLS-II Interior
    BNL NSLS-II Interior

    ANL APS interior
    ANL APS interior

    SLAC/SSRL
    SLAC/SSRL

    Organizing the transition edge sensors into arrays made a more powerful detector. The prototype sensor—built in 1995—consisted of only one pixel.

    These early detectors had poor resolution, says physicist Kent Irwin of Stanford University and SLAC. He built the original single-pixel transition edge sensor as a postdoc. Like a camera, the detector can capture greater detail the more pixels it has.

    “It’s only now that we’re hitting hundreds of pixels that it’s really getting useful,” Irwin says. “As you keep increasing the pixel count, the science you can do just keeps multiplying. And you start to do things you didn’t even conceive of being possible before.”

    Each of the 240 pixels is designed to catch a single photon at a time. These detectors are efficient, says Irwin, collecting photons that may be missed with more conventional detectors.

    Spectroscopy experiments at synchrotrons examine subtle features of matter using X-rays. In these types of experiments, an X-ray beam is directed at a sample. Energy from the X-rays temporarily excites the electrons in the sample, and when the electrons return to their lower energy state, they release photons. The photons’ energy is distinctive for a given chemical element and contains detailed information about the electronic structure.

    As the transition edge sensor captures these photons, every individual pixel on the detector functions as a high-energy-resolution spectrometer, able to determine the energy of each photon collected.

    The researchers combine data from all the pixels and make note of the pattern of detected photons across the entire array and each of their energies. This energy spectrum reveals information about the molecule of interest.

    These spectrometers are 100 times more sensitive than standard spectrometers, says Dennis Nordlund, SLAC scientist and leader of the transition edge sensor project at SSRL. This allows a look at biological and chemical details at extremely low concentrations using soft (low-energy) X-rays.

    “These technology advances mean there are many things we can do now with spectroscopy that were previously out of reach,” Nordlund says. “With this type of sensitivity, this is when it gets really interesting for chemistry.”

    The early experiments at Brookhaven looked at bonding and the chemical structure of nitrogen-bearing explosives. With the spectrometer at Argonne, a research team recently took scattering measurements on high-temperature superconducting materials.

    “The instruments are very similar from a technical standpoint—same number of sensors, similar resolution and performance,” Swetz says. “But it’s interesting, the labs are all doing different science with the same basic equipment.”

    At NIST, Swetz says they’re working to pair these detectors with less intense light sources, which could enable researchers to do X-ray experiments in their personal labs.

    There are plans to build transition-edge-sensor spectrometers that will work in the higher energy hard X-ray region, which scientists at Argonne are working on for the next upgrade of Advanced Photon Source.

    To complement this, the SLAC and NIST collaboration is engineering spectrometers that will handle the high repetition rate of X-ray laser pulses such as LCLS-II, the next generation of the free-electron X-ray laser at SLAC. This will require faster readout systems. The goal is to create a transition-edge-sensor array with as many as 10,000 pixels that can capture more than 10,000 pulses per second.

    Irwin points out that the technology developed for synchrotrons, LCLS-II and future cosmic-microwave-background experiments provides shared benefit.

    “The information really keeps bouncing back and forth between X-ray science and cosmology,” Irwin says

    See the full article here .

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    Symmetry is a joint Fermilab/SLAC publication.


     
  • richardmitnick 8:27 pm on January 5, 2017 Permalink | Reply
    Tags: A New Way to See Proteins in Motion, ANL APS, , EF-X (electric field-stimulated x-ray crystallography), X-ray images of proteins,   

    From ANL APS: “A New Way to See Proteins in Motion” 

    ANL Lab

    News APS at Argonne National Laboratory

    01.03.2017
    No writer credit

    1
    A new technique to watch proteins in action involves applying large voltage pulses to protein crystals simultaneously with x-ray pulses, as shown in the photo (at left) of the experimental set-up in the BioCARS beamline at the APS. At right is a close-up view of a crystal sandwiched between electrodes that deliver the voltage.

    University of Texas Southwestern Medical Center researchers, in conjunction with colleagues from the University of Chicago, have developed a new imaging technique that makes x-ray images of proteins as they move in response to electric field pulses. The method could lead to new insights into how proteins work, said senior author Dr. Rama Ranganathan, of UT Southwestern. The technique had its first application in experiments at the U.S. Department of Energy Office of Science’s Advanced Photon Source (APS) at Argonne National Laboratory. The results were published in Nature.

    “Proteins carry out the basic reactions in cells that are necessary for life: They bind to other molecules, catalyze chemical reactions, and transmit signals within the cell,” said Ranganathan. “These actions come from their internal mechanics; that is, from the coordinated motions of the network of amino acids that make up the protein.”

    Often, Ranganathan said, the motions that underlie protein function are subtle and happen on time scales ranging from trillionths of a second to many seconds.

    “So far, we have had no direct way of ‘seeing’ the motions of amino acids over this range and with atomic precision, which has limited our ability to understand, engineer, and control proteins,” he said.

    The new method, which the researchers call EF-X (electric field-stimulated x-ray crystallography), is aimed at stimulating motions within proteins and visualizing those motions in real time at atomic resolution, he said. This approach makes it possible to create video-like images of proteins in action – a goal of future research, he explained.

    The method involves subjecting proteins to large electric fields of about 1 million volts per centimeter and simultaneously reading out the effects with x-ray crystallography, he said.

    The researchers’ EF-X experiments utilizing the BioCARS 14-ID x-ray beamline at the APS, which is an Office of Science user facility, showed proteins can sustain these intense electric fields, and further that the imaging method can expose the pattern of shape changes associated with a protein’s function. Additional standard crystallography data (in the absence of electric field) were collected at beamline 11-1, at Stanford Synchrotron Radiation Lightsource at the SLAC National Accelerator laboratory, also an Office of Science user facility.

    SLAC/SSRL
    SLAC/SSRL

    “This is not the first report of seeing atomic motions in proteins, but previous reports were specialized for particular proteins and particular kinds of motions,” said Ranganathan. “Our work is the first to open up the investigation to potentially all possible motions, and for any protein that can be crystallized. It changes what we can learn.”

    Ultimately, this work could explain how proteins work in both normal and disease states, with implications in protein engineering and drug discovery. An immediate goal is to make the method simple enough for other researchers to use, he added.

    “I think this work has opened a new door to understanding protein function. It is already capable of being used broadly for many very important problems in biology and medicine. But like any new method, there is room for many improvements that will come from both us and others. The first step will be to create a way for other scientists to use this method for themselves,” Ranganathan said.

    The group reports that they used the technique to study the PDZ domain of the human ubiquitin ligase protein LNX2, and found new information regarding how the protein actually works.

    See: Doeke R. Hekstra1‡, K. Ian White1, Michael A. Socolich1, Robert W. Henning2, Vukica Šrajer2, and Rama Ranganathan1*, Electric-field-stimulated protein Mechanics, Nature 540, 400 (15 December 2016). DOI: 10.1038/nature20571

    Author affiliations: 1. UT Southwestern Medical Center, 2. The University of Chicago ‡ Present address: Harvard University

    Correspondence: *rama.ranganathan@utsouthwestern.edu

    See the full article here .

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    Argonne is managed by UChicago Argonne, LLC for the U.S. Department of Energy’s Office of Science

    The Advanced Photon Source at Argonne National Laboratory is one of five national synchrotron radiation light sources supported by the U.S. Department of Energy’s Office of Science to carry out applied and basic research to understand, predict, and ultimately control matter and energy at the electronic, atomic, and molecular levels, provide the foundations for new energy technologies, and support DOE missions in energy, environment, and national security.

    Argonne Lab Campus
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  • richardmitnick 7:04 am on September 1, 2016 Permalink | Reply
    Tags: ANL APS, , Cement, ,   

    From Princeton: Women in STEM – “Claire White receives National Science Foundation grant to study green cement” 

    Princeton University
    Princeton University

    9.1.16
    Sharon Adarlo

    1
    Claire White

    Claire White, an assistant professor of civil and environmental engineering and the Andlinger Center for Energy and the Environment at Princeton University, received a five-year CAREER grant from the National Science Foundation (NSF) to investigate more sustainable and resilient alternatives to Portland cement, a fundamental constituent in concrete and whose production emits one ton of carbon dioxide for every ton produced, accounting for five to eight percent of global carbon-dioxide emissions.

    The NSF supports junior faculty members, such as White, “who exemplify the role of teacher-scholars through outstanding research, excellent education, and the integration of education and research within the context of the mission of their organizations,” through their Faculty Early Career Development Program, according to the NSF website.

    With this grant, White and her research group will look at the long term durability of alternative cement binders made from blast furnace slag (also known as alkali-activated slag), a glass-like material that is a byproduct of steel production. Blast furnace slag is already recycled for use in concrete in order to reduce the amount of Portland cement powder used, but it can replace all the Portland cement needed in a batch of concrete via a chemical activation process, further reducing greenhouse emissions.

    Both Portland cement binder and alkali-activated slag binder have been shown to be equally strong, but the slag binder’s long term durability has not yet been fully determined – including when exposed to atmospheric carbon dioxide. The slag binder degrades in the presence of carbon dioxide in a process known as carbonation. This grant will allow White to investigate multiple types of alkali-activated slag, discover which among them is more resistant to carbonation, and understand the underlying chemistries of the materials.

    “This research is so important because making Portland cement powder is detrimental to the environment. A significant amount of carbon dioxide is released into the atmosphere as a result of mining, producing, and transporting the material,” she said. “Finding durable alternatives will be crucial in order to make a large dent in reducing the amount of greenhouse gases we are releasing into the atmosphere.”

    Being a byproduct of steel production, the properties of the slag, White explains, depend much on the mineral composition of iron ore that was used and the specific conditions used during the production of cast iron, which is a part of the steel manufacturing process.

    “We get slag from different locations: New Jersey, Canada, and overseas,” she said. “It’s important to look at slag from different countries or plants because the material’s properties differ from one place to another.”

    Before securing the grant, White and her team had already done preliminary work that found some alkali-activated slags to be more resistant to carbonation than other types of alkali-activated slag. This previous research was funded by a grant from Princeton E-ffiliates Partnership, a corporate affiliates program administered by the Andlinger Center.

    “We really want to understand why certain slags work better than others in these alkali-activated cements. And then we want to exploit the processes on why this good slag works, so we can tailor the materials to be even more resistant to carbon dioxide,” she said.

    For the study, White and her team plan to visit Argonne National Laboratory, just outside Chicago, in order to use the facility’s high-end synchrotron, a special piece of equipment, to perform experiments.

    ANL APS
    ANL APS interior
    ANL APS

    The synchrotron experiments will enable the team to track in high resolution the structural changes of the alkali-activated slag binder as it undergoes carbonation in real time – a process they can’t measure on campus.

    “It is crucial to determine what changes happen to the fundamental atomic structures,” White said about carbonation. “We need to apply state-of-art techniques to these materials in order to figure out the fundamental mechanisms that occur during exposure to carbon dioxide.”

    Though the grant only covers alkali-activated slag, White’s investigations may yield insight into other alternatives to Portland cement, such as fly ash, a coal burning byproduct, and ash derived from municipal solid-waste incineration.

    “Slag-based alkali-activated concrete is just one solution to reduce carbon dioxide in the environment due to concrete production,” she said. “Once we understand what’s going on in slag systems, we can look at other waste byproducts that could be just as useful as slag.”

    As part of the grant, White will also put together an educational component for teachers who want to incorporate engineering into their curriculum. White said she will put together lesson plans and teaching modules on how cement and related construction materials are used in a variety of engineering applications, and how engineers are critical for solving climate change.

    “Educating the next generation of engineers and scientists is so important,” she said. “I am glad I am part of this effort.”

    White earned bachelor degrees in civil engineering and physics from the University of Melbourne, Australia in 2006. She then earned her doctorate in chemical engineering from Melbourne as well in 2010. She joined the Andlinger Center in 2013 and is also an associate faculty member in the Department of Chemical and Biological Engineering and the Princeton Institute for the Science and Technology of Materials (PRISM). She was previously a Director’s postdoctoral fellow at the Los Alamos National Laboratory in Los Alamos, New Mexico.

    The mission of the Andlinger Center for Energy and the Environment (ACEE) is to develop solutions to ensure our energy and environmental future. To this end, the center supports a vibrant and expanding program of research and teaching in the areas of sustainable energy-technology development, energy efficiency, and environmental protection and remediation. A chief goal of the center is to translate fundamental knowledge into practical solutions that enable sustainable energy production and the protection of the environment and global climate from energy-related anthropogenic change.

    For more information on the Andlinger Center for Energy and the Environment at Princeton University, contact Sharon Adarlo, communications specialist, at sadarlo@princeton.edu or (609) 258-9979.

    See the full article here .

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    As a world-renowned research university, Princeton seeks to achieve the highest levels of distinction in the discovery and transmission of knowledge and understanding. At the same time, Princeton is distinctive among research universities in its commitment to undergraduate teaching.

    Today, more than 1,100 faculty members instruct approximately 5,200 undergraduate students and 2,600 graduate students. The University’s generous financial aid program ensures that talented students from all economic backgrounds can afford a Princeton education.

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  • richardmitnick 11:40 am on August 2, 2016 Permalink | Reply
    Tags: ANL APS, , , , ,   

    From Chicago Tribune via ANL: “This giant X-ray machine helped decode one of the Zika virus’ secrets “ 

    Argonne Lab

    News from Argonne National Laboratory

    1

    Chicago Tribune

    8.2.16
    Ally Marotti

    2
    Other viruses in the same family as Zika, such as dengue, West Nile and yellow fever, also produce the NS1 protein. (Argonne National Laboratory)

    A group of Midwest researchers is one step closer to a Zika vaccine, and they used a giant X-ray machine at the Chicago area’s Argonne National Lab to get there.

    University of Michigan and Purdue University researchers used equipment at Lemont-based Argonne to map the molecular structure of a protein the Zika virus produces.

    That knowledge can lead to more accurate diagnoses of Zika and possibly a vaccine or antiviral drugs, said Janet Smith, professor of biological chemistry in the Life Sciences Institute at Michigan.

    “We don’t have good diagnostic tools to know if a person has been infected with Zika,” said Smith, who led the study. “There are a bunch of antibody tests out there to see if you’ve been exposed to Zika — the problem is they’re not specific enough.”

    Of course no vaccine will come in time for the Olympics, which start next week, Smith said, but these findings are important in the fight against the disease.

    Zika is a growing concern in the U.S., as cases are increasingly reported in countries outside of the tropics. The virus is known to cause devastating birth defects, and the World Health Organization declared an international health emergency over its spread.

    Nearly 1,500 cases have been reported in the U.S., according to the Centers for Disease Control and Prevention, but all were acquired while traveling. However, experts say that will change by the end of the year.

    Although a study out of Yale University found it’s highly unlikely those traveling to Rio de Janeiro for the Olympics will contract the disease, fear has amplified as the games approach.

    The protein Smith and her team looked at is called NS1. Other viruses in the same family as Zika, such as dengue, West Nile and yellow fever, also produce the protein. When a person gets infected, the virus induces their body to make the protein.

    “It helps the virus to make more copies of itself, infect (the body’s) cells and hide from the immune system in ways that are really not very well understood at all,” Smith said.

    Since Zika is a problem in places where dengue fever is prevalent, inaccurate diagnoses sometimes prevent people from knowing which disease they were exposed to. These new findings will hopefully change that, Smith said.

    The researchers used Argonne’s Advanced Photon Source to conduct the study. The facility is used to conduct X-ray research, and is so large that its diameter measures just a little less than the height of the Willis Tower, said Stephen Streiffer, director of the facility.

    “APS is used to produce hard X-rays — the same type you’d get in the dentist’s office,” Streiffer said. “The difference is that the APS produces X-rays which are about a billion times more intense.”

    Smith and her team made a stable NS1 protein from Zika and put it into a crystal, which scatters the X-ray beam. Smith’s team uses a detector to measure the scattering, and can then figure out the structure of the molecule inside.

    The researchers had already been studying structures of the proteins from West Nile and dengue, so that sped up the process, Smith said. Richard Kuhn, professor and head of Purdue’s Department of Biological Sciences, co-authored the study, which was published Monday in the journal Nature Structural & Molecular Biology.

    The protein they looked at was from the first strain of Zika identified in Uganda in 1947, Smith said. Knowing its structure can help scientists understand how the virus has mutated since it spread to Brazil.

    “Has it gotten worse when it evolved on its way to Brazil, or has it been this bad all along?” Smith said. “Viruses are amazing at sneaking around mutating … It’s like cancer. They produce fast and make a bunch of mistakes, but just one needs to take off.

    See the full article here .

    YOU CAN HELP FIND A CURE FOR THE ZIKA VIRUS.

    There is a new project at World Community Grid [WCG] called OpenZika.
    Zika
    Image of the Zika virus, Image copyright John Liebler, http://www.ArtoftheCell.com
    Rutgers Open Zika

    WCG runs on your home computer or tablet on software from Berkeley Open Infrastructure for Network Computing [BOINC]. Many other scientific projects run on BOINC software.Visit WCG or BOINC, download and install the software, then at WCG attach to the OpenZika project. You will be joining tens of thousands of other “crunchers” processing computational data and saving the scientists literally thousands of hours of work at no real cost to you.

    This project is directed by Dr. Alexander Perryman a senior researcher in the Freundlich lab, with extensive training in developing and applying computational methods in drug discovery and in the biochemical mechanisms of multi-drug-resistance in infectious diseases. He is a member of the Center for Emerging & Re-emerging Pathogens, in the Department of Pharmacology, Physiology, and Neuroscience, at the Rutgers University, New Jersey Medical School. Previously, he was a Research Associate in Prof. Arthur J. Olson’s lab at The Scripps Research Institute (TSRI), where he ran the day-to-day operations of the FightAIDS@Home project, the largest computational drug discovery project devoted to HIV/AIDS, which also runs on WCG. While in the Olson lab, he also designed, led, and ran the largest computational drug discovery project ever performed against malaria, the GO Fight Against Malaria project, also on WCG.

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    Argonne National Laboratory seeks solutions to pressing national problems in science and technology. The nation’s first national laboratory, Argonne conducts leading-edge basic and applied scientific research in virtually every scientific discipline. Argonne researchers work closely with researchers from hundreds of companies, universities, and federal, state and municipal agencies to help them solve their specific problems, advance America’s scientific leadership and prepare the nation for a better future. With employees from more than 60 nations, Argonne is managed by UChicago Argonne, LLC for the U.S. Department of Energy’s Office of Science. For more visit http://www.anl.gov.

    The Advanced Photon Source at Argonne National Laboratory is one of five national synchrotron radiation light sources supported by the U.S. Department of Energy’s Office of Science to carry out applied and basic research to understand, predict, and ultimately control matter and energy at the electronic, atomic, and molecular levels, provide the foundations for new energy technologies, and support DOE missions in energy, environment, and national security. To learn more about the Office of Science X-ray user facilities, visit http://science.energy.gov/user-facilities/basic-energy-sciences/.

    Argonne is managed by UChicago Argonne, LLC for the U.S. Department of Energy’s Office of Science

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  • richardmitnick 7:05 am on July 29, 2016 Permalink | Reply
    Tags: ANL APS, , , ,   

    From Chicago Tribune via ANL: “This giant X-ray machine helped decode one of the Zika virus’ secrets” 

    ANL APS
    News from Argonne National Laboratory
    Advanced Photon Source at ANL

    1

    http://www.chicagotribune.com

    7.26.16
    Ally Marotti

    A group of Midwest researchers is one step closer to a Zika vaccine, and they used a giant X-ray machine at the Chicago area’s Argonne National Lab to get there.

    University of Michigan and Purdue University researchers used equipment at Lemont-based Argonne to map the molecular structure of a protein the Zika virus produces.

    That knowledge can lead to more accurate diagnoses of Zika and possibly a vaccine or antiviral drugs, said Janet Smith, professor of biological chemistry in the Life Sciences Institute at Michigan.

    “We don’t have good diagnostic tools to know if a person has been infected with Zika,” said Smith, who led the study. “There are a bunch of antibody tests out there to see if you’ve been exposed to Zika — the problem is they’re not specific enough.”

    Of course no vaccine will come in time for the Olympics, which start next week, Smith said, but these findings are important in the fight against the disease.

    Zika is a growing concern in the U.S., as cases are increasingly reported in countries outside of the tropics. The virus is known to cause devastating birth defects, and the World Health Organization declared an international health emergency over its spread.

    Nearly 1,500 cases have been reported in the U.S., according to the Centers for Disease Control and Prevention, but all were acquired while traveling. However, experts say that will change by the end of the year.

    Although a study out of Yale University found it’s highly unlikely those traveling to Rio de Janeiro for the Olympics will contract the disease, fear has amplified as the games approach.

    The protein Smith and her team looked at is called NS1. Other viruses in the same family as Zika, such as dengue, West Nile and yellow fever, also produce the protein. When a person gets infected, the virus induces their body to make the protein.

    “It helps the virus to make more copies of itself, infect (the body’s) cells and hide from the immune system in ways that are really not very well understood at all,” Smith said.

    Since Zika is a problem in places where dengue fever is prevalent, inaccurate diagnoses sometimes prevent people from knowing which disease they were exposed to. These new findings will hopefully change that, Smith said.

    The researchers used Argonne’s Advanced Photon Source to conduct the study. The facility is used to conduct X-ray research, and is so large that its diameter measures just a little less than the height of the Willis Tower, said Stephen Streiffer, director of the facility.

    “APS is used to produce hard X-rays — the same type you’d get in the dentist’s office,” Streiffer said. “The difference is that the APS produces X-rays which are about a billion times more intense.”

    Smith and her team made a stable NS1 protein from Zika and put it into a crystal, which scatters the X-ray beam. Smith’s team uses a detector to measure the scattering, and can then figure out the structure of the molecule inside.

    The researchers had already been studying structures of the proteins from West Nile and dengue, so that sped up the process, Smith said. Richard Kuhn, professor and head of Purdue’s Department of Biological Sciences, co-authored the study, which was published Monday in the journal “Nature Structural & Molecular Biology.”

    The protein they looked at was from the first strain of Zika identified in Uganda in 1947, Smith said. Knowing its structure can help scientists understand how the virus has mutated since it spread to Brazil.

    “Has it gotten worse when it evolved on its way to Brazil, or has it been this bad all along?” Smith said. “Viruses are amazing at sneaking around mutating … It’s like cancer. They produce fast and make a bunch of mistakes, but just one needs to take off.”

    See the full article here .

    YOU CAN HELP FIND A CURE FOR THE ZIKA VIRUS.

    There is a new project at World Community Grid [WCG] called OpenZika.
    Zika
    Image of the Zika virus

    Rutgers Open Zika

    WCG runs on your home computer or tablet on software from Berkeley Open Infrastructure for Network Computing [BOINC]. Many other scientific projects run on BOINC software.Visit WCG or BOINC, download and install the software, then at WCG attach to the OpenZika project. You will be joining tens of thousands of other “crunchers” processing computational data and saving the scientists literally thousands of hours of work at no real cost to you.

    This project is directed by Dr. Alexander Perryman a senior researcher in the Freundlich lab, with extensive training in developing and applying computational methods in drug discovery and in the biochemical mechanisms of multi-drug-resistance in infectious diseases. He is a member of the Center for Emerging & Re-emerging Pathogens, in the Department of Pharmacology, Physiology, and Neuroscience, at the Rutgers University, New Jersey Medical School. Previously, he was a Research Associate in Prof. Arthur J. Olson’s lab at The Scripps Research Institute (TSRI), where he ran the day-to-day operations of the FightAIDS@Home project, the largest computational drug discovery project devoted to HIV/AIDS, which also runs on WCG. While in the Olson lab, he also designed, led, and ran the largest computational drug discovery project ever performed against malaria, the GO Fight Against Malaria project, also on WCG.

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    Please help promote STEM in your local schools.
    STEM Icon
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    Argonne National Laboratory seeks solutions to pressing national problems in science and technology. The nation’s first national laboratory, Argonne conducts leading-edge basic and applied scientific research in virtually every scientific discipline. Argonne researchers work closely with researchers from hundreds of companies, universities, and federal, state and municipal agencies to help them solve their specific problems, advance America’s scientific leadership and prepare the nation for a better future. With employees from more than 60 nations, Argonne is managed by UChicago Argonne, LLC for the U.S. Department of Energy’s Office of Science. For more visit http://www.anl.gov.

    The Advanced Photon Source at Argonne National Laboratory is one of five national synchrotron radiation light sources supported by the U.S. Department of Energy’s Office of Science to carry out applied and basic research to understand, predict, and ultimately control matter and energy at the electronic, atomic, and molecular levels, provide the foundations for new energy technologies, and support DOE missions in energy, environment, and national security. To learn more about the Office of Science X-ray user facilities, visit http://science.energy.gov/user-facilities/basic-energy-sciences/.

    Argonne is managed by UChicago Argonne, LLC for the U.S. Department of Energy’s Office of Science

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