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<title>Phys.org: Phys.Org news tagged with: crystallography</title>
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<description>Phys.org internet news portal provides the latest news on science including: Physics, Nanotechnology, Life Sciences, Space Science, Earth Science, Environment, Health and Medicine.</description>

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     <title>Iron-sulfur enzymes as candidates for antibiotic development</title>
   	 <description>The iron-sulfur protein IspH plays a central role in the terpene metabolism of several pathogens. The mechanism of the reaction provides an approach for developing new antibiotics, particularly against malaria and tuberculosis. While researching this enzyme, biochemists at the Technische Universitat Munchen discovered a previously unknown reaction: IspH accepts two completely different classes of molecules as partners. This surprising insight, published in Nature Communications, opens up new perspectives in combating infectious diseases.</description>
     <link>http://phys.org/news269001944.html</link>
	 <category>Chemistry</category>
	 <pubDate>Tue, 09 Oct 2012 11:45:52 EST</pubDate>
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     <title>Protein structure unlocks one mystery of multi-drug tolerance</title>
   	 <description>The structures of key bacterial proteins have revealed one of the biochemical secrets that enables bacteria to outwit antibiotics.</description>
     <link>http://phys.org/news267883375.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 26 Sep 2012 13:03:11 EST</pubDate>
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     <title>Making a molecular micromap: Imaging the yeast 26S proteasome at near-atomic resolution</title>
   	 <description>(Phys.org)—Biological systems are characterized by a form of molecular recycling – and proteins do not escape this fate. In particular, unneeded or damaged proteins biochemically marked for destruction undergo controlled degradation by having their peptide bonds broken by proteasomes. Recently, scientists at the Max-Planck Institute of Biochemistry in Germany used cryo-electron microscopy (cryo-EM) single particle analysis and molecular dynamics techniques to map the Saccharomyces cerevisiae 26S proteasome. (Cryo-EM is a form of transmission electron microscopy where the sample is studied at cryogenic temperatures, which unlike X-ray crystallography allows researchers to observe specimens in their native environment without the need for staining or fixing. S. cerevisiae is the yeast species commonly known as baker's or brewer's yeast.) The researchers then used this map to build a near-atomic resolution structural model of the proteasome. The Max Planck team showed that cryo-electron microscopy allowed them to successfully model the 26S core complex where X-ray crystallography studies conducted over the past 20 years have not. </description>
     <link>http://phys.org/news267682061.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 24 Sep 2012 08:30:01 EST</pubDate>
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     <title>Intrinsically disordered proteins: A conversation with Rohit Pappu</title>
   	 <description>If you open any biology textbook to the section on proteins, you will learn that a protein is made up of a sequence of amino acids, that the sequence determines how the chain of amino acids folds into a compact structure, and that the folded protein's structure determines its function. In other words sequence encodes structure and function derives from structure.</description>
     <link>http://phys.org/news267368532.html</link>
	 <category>Biology</category>
	 <pubDate>Thu, 20 Sep 2012 14:02:33 EST</pubDate>
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     <title>Small is beautiful: Viewing hydrogen atoms with neutron protein crystallography</title>
   	 <description>(Phys.org)—Creating 3D visualizations of hydrogen atoms in proteins is especially challenging, often requiring their locations to be inferred from those of nearby carbon, nitrogen, oxygen or sulfur atoms stored in protein structure databases. These locations are based on atomic positions in databases of previously solved structures, general chemical knowledge, quantum mechanical calculations, or potential hydrogen bonding interactions. While X-ray crystallography can pinpoint hydrogen atom locations at ultrahigh resolution, in practice only a few such positions are experimentally determined. Recently, however, scientists at the University of Toledo, Los Alamos National Laboratory and Oak Ridge National Laboratory used neutron crystallography – a technique that even at lower resolutions can locate individual hydrogen atoms by leveraging scattering properties of the hydrogen isotope deuterium. </description>
     <link>http://phys.org/news267348141.html</link>
	 <category>Physics</category>
	 <pubDate>Thu, 20 Sep 2012 09:10:01 EST</pubDate>
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     <title>Revelation of protein complex function that controls cell proliferation in fruit fly wings provides insights into tumor </title>
   	 <description>A team of researchers in Singapore has determined the structure of a pair of proteins that may play an important role in tumor growth and the progression of cancer. The proteins, Vestigial (Vg) and Scalloped (Sd), normally control wing development in fruit flies, but the team found they show a remarkable structural and functional similarity to the cancer-promoting proteins called YAP and TAZ.</description>
     <link>http://phys.org/news266658464.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 12 Sep 2012 09:00:12 EST</pubDate>
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     <title>A new approach for solving protein structures</title>
   	 <description>(Phys.org)—Using synchrotron x-ray beams to solve the molecular structures of proteins and other large biological molecules has yielded many advances in medicine, such as drug therapies for cancer. Improvements in the techniques available to scientists could lead to even more exciting advances. Recently, scientists from NSLS, the New York Structural Biology Center and Columbia University discovered a new method to determine molecular structures that would have been difficult or impossible to solve otherwise. Their work is reported in the May 25 online edition of Science.</description>
     <link>http://phys.org/news266139713.html</link>
	 <category>Physics</category>
	 <pubDate>Thu, 06 Sep 2012 08:42:22 EST</pubDate>
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     <title>Delving into the molecular mechanism behind deep-sea bacteria's pressure tolerance</title>
   	 <description>The Mariana Trench is the deepest feature of the Earth's surface. The water column there exerts a pressure of more than one thousand times normal atmospheric pressure at sea level, enough pressure to crush an SUV. Yet many organisms thrive in this seemingly inhospitable environment. A Japanese research team has been investigating how deep-sea bacteria adapt to such high-pressure conditions. They have identified a structural change that confers pressure-resistant properties on a particular protein found in bacteria. </description>
     <link>http://phys.org/news262514500.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 26 Jul 2012 09:41:45 EST</pubDate>
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     <title>Scientists solve structure of important protein in energy storage of cells</title>
   	 <description>(Phys.org) -- Scientists at Trinity College Dublin, using a highly specialised crystallography technique have solved a large protein structure that will increase our understanding of energy generation and storage in cells. The findings have been recently published in the online publication of Nature.</description>
     <link>http://phys.org/news261806876.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 18 Jul 2012 05:08:03 EST</pubDate>
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     <title>Combining crystallography and visible spectroscopy to understand enzymes</title>
   	 <description>Structure and function are intimately linked, but do not necessarily predict the other. For example, x-ray crystallography provides 3D atomic structural information about biological macromolecules but does not define important details about metal ions.</description>
     <link>http://phys.org/news260159929.html</link>
	 <category>Chemistry</category>
	 <pubDate>Fri, 29 Jun 2012 03:39:13 EST</pubDate>
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     <title>Researchers establishe structure of a new superhard form of carbon</title>
   	 <description>(Phys.org) -- An international team led by Artem R. Oganov, PhD, a professor of theoretical crystallography in the Department of Geosciences at Stony Brook University, has established the structure of a new form of carbon. The results of their work, &amp;#147;Understanding the Nature of Superhard Graphite,&amp;#148; were published June 26 in Scientific Reports, a new journal of the Nature Publishing Group.</description>
     <link>http://phys.org/news260006319.html</link>
	 <category>Nanotechnology</category>
	 <pubDate>Wed, 27 Jun 2012 08:58:59 EST</pubDate>
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     <title>Atomic-resolution view of a receptor reveals how stomach bacterium avoids acid</title>
   	 <description>University of Oregon scientists have discovered how the bacterium Helicobacter pylori navigates through the acidic stomach, opening up new possibilities to inactivate its disease-causing ability without using current strategies that often fail or are discontinued because of side effects.</description>
     <link>http://phys.org/news258897008.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 14 Jun 2012 12:50:24 EST</pubDate>
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     <title>SLAC X-ray laser used to probe biomolecules to individual atoms</title>
   	 <description>An international team led by SLAC National Accelerator Laboratory has proved how the world's most powerful X-ray laser can assist in cracking the structures of biomolecules, and in the processes helped to pioneer critical new investigative avenues in biology.</description>
     <link>http://phys.org/news257689199.html</link>
	 <category>Physics</category>
	 <pubDate>Thu, 31 May 2012 14:00:16 EST</pubDate>
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     <title>Discarded data may hold the key to a sharper view of molecules</title>
   	 <description>(Phys.org) -- There's nothing like a new pair of eyeglasses to bring fine details into sharp relief. For scientists who study the large molecules of life from proteins to DNA, the equivalent of new lenses have come in the form of an advanced method for analyzing data from X-ray crystallography experiments.</description>
     <link>http://phys.org/news257078826.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 24 May 2012 14:00:10 EST</pubDate>
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     <title>MIT biologist relishes the challenge of picking apart the cell's most complex structure</title>
   	 <description>One of the most important structures in a cell is the nuclear pore complex &amp;#151; a tiny yet complicated channel through which information flows in and out of the cell&amp;#146;s nucleus, directing all other cell activity.</description>
     <link>http://phys.org/news256883870.html</link>
	 <category>Biology</category>
	 <pubDate>Tue, 22 May 2012 05:39:04 EST</pubDate>
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     <title>Scientists learn how to 'out run damage' with imaging technique</title>
   	 <description>Over the decades X-ray crystallography has been fundamental in the development of many scientific fields. The method has revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. However, in order to obtain good data, large single crystals are required. These are often nearly impossible to grow. There also is the problem that X-rays damage delicate biological samples.</description>
     <link>http://phys.org/news249041525.html</link>
	 <category>Physics</category>
	 <pubDate>Tue, 21 Feb 2012 10:14:50 EST</pubDate>
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     <title>Fastest X-ray images of tiny biological crystals</title>
   	 <description>(PhysOrg.com) -- An international research team headed by DESY scientists from the Center for Free-Electron Laser Science (CFEL) in Hamburg, Germany, has recorded the shortest X-ray exposure of a protein crystal ever achieved. The incredible brief exposure time of 0.000 000 000 000 03 seconds (30 femtoseconds) opens up new possibilities for imaging molecular processes with X-rays. This is of particular interest to biologists, but can be employed in many fields, explain lead authors Dr. Anton Barty and Prof. Henry Chapman from the German accelerator centre Deutsches Elektronen-Synchrotron DESY. </description>
     <link>http://phys.org/news244977149.html</link>
	 <category>Physics</category>
	 <pubDate>Thu, 05 Jan 2012 09:12:44 EST</pubDate>
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     <title>Scientists study protein dynamical transitions</title>
   	 <description>(PhysOrg.com) -- Central to life and all cellular functions, proteins are complex structures that are anything but static, though often illustrated as two-dimensional snapshots in time.</description>
     <link>http://phys.org/news243156876.html</link>
	 <category>Biology</category>
	 <pubDate>Thu, 15 Dec 2011 07:50:04 EST</pubDate>
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     <title>New strategy could lead to dose reduction in X-ray imaging</title>
   	 <description>For more than a century, the use of X-rays has been a prime diagnostic tool when it comes to human health. As it turns out, X-rays also are a crucial component for studying and understanding molecules, and a new approach -- just published by researchers at the University of Georgia -- may dramatically improve what researchers can learn using the technique.</description>
     <link>http://phys.org/news241178212.html</link>
	 <category>Physics</category>
	 <pubDate>Tue, 22 Nov 2011 10:30:01 EST</pubDate>
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     <title>SLAC X-rays help discover new drug against melanoma</title>
   	 <description>It was front page news around the world: a drug designed to disrupt malignant melanoma, the deadliest form of skin cancer, was so successful in its latest round of testing in humans that the tests were halted &amp;#150; like an early-round knockout in boxing &amp;#150; so patients in the trial who were receiving other treatments could be moved to the new medicine.</description>
     <link>http://phys.org/news230289978.html</link>
	 <category>Chemistry</category>
	 <pubDate>Tue, 19 Jul 2011 10:26:39 EST</pubDate>
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     <title>Narrowest bridges of gold are also the strongest, study finds</title>
   	 <description>At an atomic scale, the tiniest bridge of gold -- that made of a single atom -- is actually the strongest, according to new research by engineers at the University at Buffalo's Laboratory for Quantum Devices.</description>
     <link>http://phys.org/news229788092.html</link>
	 <category>Nanotechnology</category>
	 <pubDate>Wed, 13 Jul 2011 15:01:41 EST</pubDate>
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     <title>Hitting moving RNA drug targets</title>
   	 <description>By accounting for the floppy, fickle nature of RNA, researchers at the University of Michigan and the University of California, Irvine have developed a new way to search for drugs that target this important molecule. Their work appears in the June 26 issue of Nature Chemical Biology.</description>
     <link>http://phys.org/news228324745.html</link>
	 <category>Chemistry</category>
	 <pubDate>Sun, 26 Jun 2011 16:32:43 EST</pubDate>
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     <title>Boosting research into new drugs: 'Smart materials' make proteins form crystals</title>
   	 <description>Scientists have developed a new method to make proteins form crystals using 'smart materials' that remember the shape and characteristics of the molecule. The technique, reported today in Proceedings of the National Academy of Sciences, should assist research into new medicines by helping scientists work out the structure of drug targets.</description>
     <link>http://phys.org/news227792882.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 20 Jun 2011 15:00:21 EST</pubDate>
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     <title>Lasers used to form 3-D crystals made of nanoparticles (w/ video)</title>
   	 <description>(PhysOrg.com) -- University of Michigan physicists used the electric fields generated by intersecting laser beams to trap and manipulate thousands of microscopic plastic spheres, thereby creating 3-D arrays of optically induced crystals.</description>
     <link>http://phys.org/news226136384.html</link>
	 <category>Physics</category>
	 <pubDate>Wed, 01 Jun 2011 08:40:27 EST</pubDate>
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     <title>Nature's elegant solution to repairing DNA in cancer, other conditions</title>
   	 <description>A major discovery about an enzyme's structure has opened a window on understanding DNA repair. Scientists at Duke University Medical Center have determined the structure of a nuclease that will help scientists to understand several DNA repair pathways, a welcome development for cancer research.</description>
     <link>http://phys.org/news222516627.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 20 Apr 2011 11:10:49 EST</pubDate>
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     <title>The development of better biotech enzymes</title>
   	 <description>Enzymes are proteins that speed up chemical reactions, such as laundry detergent digesting protein stains, which are otherwise very difficult to remove. A research team led by Professor Kam-bo Wong of the Centre for Protein Science and Crystallography, School of Life Sciences at The Chinese University of Hong Kong demonstrated a fundamental principle in changing the activity of enzymes by means of protein engineering. The findings provide potential insights into the future design of biotechnologically important enzymes, and will be published in next week's issue of the online, open access journal PLoS Biology.</description>
     <link>http://phys.org/news219428188.html</link>
	 <category>Biology</category>
	 <pubDate>Tue, 15 Mar 2011 17:16:42 EST</pubDate>
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     <title>Researchers get a grip on nervous system's receptors</title>
   	 <description>A digital signal processing technique long used by statisticians to analyze data is helping Houston scientists understand the roots of memory and learning, Alzheimer's and Parkinson's diseases and stroke.</description>
     <link>http://phys.org/news216309912.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 07 Feb 2011 14:40:13 EST</pubDate>
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     <title>Eliminating tooth decay: Breakthrough in dental plaque research</title>
   	 <description>Dutch professors Bauke Dijkstra and Lubbert Dijkhuizen have deciphered the structure and functional mechanism of the glucansucrase enzyme that is responsible for dental plaque sticking to teeth. This knowledge will stimulate the identification of substances that inhibit the enzyme. Just add that substance to toothpaste, or even sweets, and caries will be a thing of the past. The results of the research have been published this week in the journal Proceedings of the National Academy of Sciences (PNAS).</description>
     <link>http://phys.org/news210967338.html</link>
	 <category>Chemistry</category>
	 <pubDate>Tue, 07 Dec 2010 18:02:41 EST</pubDate>
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     <title>The eukaryotic ribosome unveils its structure</title>
   	 <description>One year after the Nobel Prize in chemistry was awarded for the discovery of the bacterial ribosome's atomic structure, French researchers from the Institut de Genetique et de Biologie Moleculaire et Cellulaire have determined the first structure of a eukaryotic ribosome, that of yeast. This work, published on 26 November 2010 in the journal Science, puts an end to the frantic international race to discover the structure of this imposing cellular machinery.</description>
     <link>http://phys.org/news210421606.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 01 Dec 2010 10:27:07 EST</pubDate>
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     <title>Canadian researchers 'see' how to capture CO2</title>
   	 <description>The ability to keep CO2 out of the atmosphere to help prevent climate change is a global issue. The challenge is to use materials that can capture the CO2 and easily release it for permanent storage. Researchers at the University of Calgary and University of Ottawa have provided deeper insights to CO2 capture by &quot;seeing&quot; the exact sites where CO2 is held in a capture material. Their discovery, published in prestigious journal Science, will allow scientists to design better materials to capture more CO2.</description>
     <link>http://phys.org/news207494491.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 28 Oct 2010 14:22:06 EST</pubDate>
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