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13,927 items found (0 items not approved), displaying 51 to 60.[First/Prev] 2, 3, 4, 5, 6, 7, 8, 9 [Next/Last]

Instruments / Technical Area	Publication Details	Published	Actions
	Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures Alke Meents , Sascha Gutmann , Clemens Schulze-Briese , Armin Wagner Proceedings Of The National Academy Of Sciences 107 (3), 1094-1099 DOI: 10.1073/pnas.0905481107 Open Access Show Abstract ▼ Abstract: Radiation damage is the major impediment for obtaining structural information from biological samples by using ionizing radiation such as x-rays or electrons. The knowledge of underlying processes especially at cryogenic temperatures is still fragmentary, and a consistent mechanism has not been found yet. By using a combination of single-crystal x-ray diffraction, small-angle scattering, and qualitative and quantitative radiolysis experiments, we show that hydrogen gas, formed inside the sample during irradiation, rather than intramolecular bond cleavage between non-hydrogen atoms, is mainly responsible for the loss of high-resolution information and contrast in diffraction experiments and microscopy. The experiments that are presented in this paper cover a temperature range between 5 and 160 K and reveal that the commonly used temperature in x-ray crystallography of 100 K is not optimal in terms of minimizing radiation damage and thereby increasing the structural information obtainable in a single experiment. At 50 K, specific radiation damage to disulfide bridges is reduced by a factor of 4 compared to 100 K, and samples can tolerate a factor of 2.6 and 3.9 higher dose, as judged by the increase of Rfree values of elastase and cubic insulin crystals, respectively.	Jan 2010
	Meeting Report: PhotoEmission Electron Microscopy (PEEM) Workshop at Diamond Light Source Sara Fletcher , Sarnjeet Dhesi Synchrotron Radiation News 19, 46 - 47 Synchrotron Radiation News DOI: 10.1080/08940880601065015 Show Abstract ▼ Abstract: When Diamond Light Source goes into operation in January 2007, one of the first beamlines will house a state-of-the-art PhotoEmission Electron Microscope (PEEM). On July 12 and 13, 2006, Diamond hosted a workshop to promote the wide-ranging capabilities of PEEM to the user community. An international audience enjoyed talks and discussions on interface magnetism, geological science, surface chemistry and the principles of X-ray excited PEEM.	Dec 2006
	Biomolecular Interactions of non immobilised systems by CD spectroscopy Rohanah Hussain , Giuliano Siligardi Chirality 2007	Jul 2007
	Three-dimensional imaging of strain in a single ZnO nanorod Marcus C. Newton , Stephen J. Leake , Ross Harder , Ian K. Robinson Nature Materials DOI: 10.1038/nmat2607 PMID: 20023632 Show Abstract ▼ Abstract: Nanoscale structures can be highly strained because of confinement effects and the strong influence of their external boundaries. This results in dramatically different electronic, magnetic and optical material properties of considerable utility. Third-generation synchrotron-based coherent X-ray diffraction has emerged as a non-destructive tool for three-dimensional (3D) imaging of strain and defects in crystals that are smaller than the coherence volume, typically a few cubic micrometres, of the available beams that have sufficient flux to reveal the material's structure(1). Until now, measurements have been possible only at a single Bragg point of a given crystal because of the limited ability to maintain alignment(2); it has therefore been possible to determine only one component of displacement and not the full strain tensor. Here we report key advances in our fabrication and experimental techniques, which have enabled diffraction patterns to be obtained from six Bragg reflections of the same ZnO nanocrystal for the first time. All three Cartesian components of the ion displacement field, and in turn the full nine-component strain tensor, have thereby been imaged in three dimensions.	Dec 2009
	Design of B23 Circular Dichroism beamline at Diamond Light Source Rohanah Hussain , Giuliano Siligardi	Jul 2007
	Imaging of cochlear tissue with a grating interferometer and hard X-rays Claus-Peter Richter , Stephanie Shintani-Smith , Andrew Fishman , Christian David , Christoph Rau , Ian Robinson Microscopy Research And Technique 72 (12), 902-907 DOI: 10.1002/jemt.20728 Show Abstract ▼ Abstract: This article addresses an important current development in medical and biological imaging: the possibility of imaging soft tissue at resolutions in the micron range using hard X-rays. Challenging environments, including the cochlea, require the imaging of soft tissue structure surrounded by bone. We demonstrate that cochlear soft tissue structures can be imaged with hard X-ray phase contrast. Furthermore, we show that only a thin slice of the tissue is required to introduce a large phase shift. It is likely that the phase contrast image of the soft tissue structures is sufficient to image the structures even if surrounded by bone. For the present set of experiments, structures with low-absorption contrast have been visualized using in-line phase contrast imaging and a grating interferometer. The experiments have been performed at the Advanced Photon Source at Argonne National Laboratories, a third generation source of synchrotron radiation. The source provides highly coherent X-ray radiation with high-photon flux (>1012 photons/s) at high-photon energies (5–70 keV). Radiographic and light microscopy images of the gerbil cochlear slice samples were compared. It has been determined that a 20-?m thick tissue slice induces a phase shift between 1/3? and 2/3?. Microsc. Res. Tech., 2009. © 2009 Wiley-Liss, Inc.	Dec 2009
	Protein denaturation induced by vacuum UV radiation. Rohanah Hussain , Giuliano Siligardi International Conference on Materials for Advanced Technologies 2007	Jul 2007
	Crystal structure of A(3)B(3) complex of V-ATPase from Thermus thermophilus Megan Maher , Satoru Akimoto , Momi Iwata , Koji Nagata , Yoshiko Hori , Masasuke Yoshida , Shigeyuki Yokoyama , Ken Yokoyama , So Iwata The Embo Journal 28 (23), 3771-3779 DOI: 10.1038/emboj.2009.310 Open Access Show Abstract ▼ Abstract: Vacuolar?type ATPases (V?ATPases) exist in various cellular membranes of many organisms to regulate physiological processes by controlling the acidic environment. Here, we have determined the crystal structure of the A3B3 subcomplex of V?ATPase at 2.8 Å resolution. The overall construction of the A3B3 subcomplex is significantly different from that of the ?3?3 sub?domain in FoF1?ATP synthase, because of the presence of a protruding ‘bulge’ domain feature in the catalytic A subunits. The A3B3 subcomplex structure provides the first molecular insight at the catalytic and non?catalytic interfaces, which was not possible in the structures of the separate subunits alone. Specifically, in the non?catalytic interface, the B subunit seems to be incapable of binding ATP, which is a marked difference from the situation indicated by the structure of the FoF1?ATP synthase. In the catalytic interface, our mutational analysis, on the basis of the A3B3 structure, has highlighted the presence of a cluster composed of key hydrophobic residues, which are essential for ATP hydrolysis by V?ATPases.	Nov 2009
	Effect of 4-fluoro-L-proline on the SH3 binding affinity Paolo Ruzza , Chiara Rubini , Andrea Calderan , Andrea Guiotto , Luca Cesaro , Anna M. Brunati , Arianna Donella-Deana , Rohanah Hussain , Giuliano Siligardi Peptides For Youth: The Proceedings Of The 20th American Peptide Symposium 611, 499-500 20th American Peptide Symposium DOI: 10.1007/978-0-387-73657-0_216 PMID: 19400283	Mar 2009
	Structures of alternatively spliced isoforms of human ketohexokinase Aruna Asipu , David T. Bonthron , Simon E. V. Phillips , Chi H. Trinh Acta Crystallographica Section D Biological Crystallography 65 (3), 201-211 DOI: 10.1107/S0907444908041115 PMID: 19237742 Open Access Show Abstract ▼ Abstract: A molecular understanding of the unique aspects of dietary fructose metabolism may be the key to understanding and controlling the current epidemic of fructose-related obesity, diabetes and related adverse metabolic states in Western populations. Fructose catabolism is initiated by its phosphorylation to fructose 1-phosphate, which is performed by ketohexokinase (KHK). Here, the crystal structures of the two alternatively spliced isoforms of human ketohexokinase, hepatic KHK-C and the peripheral isoform KHK-A, and of the ternary complex of KHK-A with the substrate fructose and AMP-PNP are reported. The structure of the KHK-A ternary complex revealed an active site with both the substrate fructose and the ATP analogue in positions ready for phosphorylation following a reaction mechanism similar to that of the pfkB family of carbohydrate kinases. Hepatic KHK deficiency causes the benign disorder essential fructosuria. The effects of the disease-causing mutations (Gly40Arg and Ala43Thr) have been modelled in the context of the KHK structure.	Mar 2009

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