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226 results for “X-ray Diffraction”
IODP Expedition 376 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
IODP Expedition 385 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
IODP Expedition 396 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
IODP Expedition 354 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
IODP Expedition 362 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p> <p>Updated 26 June 2020 to include additional raw data files in supplementary materials. </p>
IODP Expedition 369 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
IODP Expedition 382 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
Microdialysis on-chip crystallization of HEWL and Thaumatin and in situ X-ray diffraction studies
<p>This deposition includes the mtz and pdb files for HEWL and Thaumatin crystal structures included in the article "Microdialysis on-chip crystallization of soluble and membrane proteins with the MicroCrys platform and in situ X-ray diffraction case studies". </p>
IODP Expedition 392 X-ray diffraction (XRD)
<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>
Raw Data: Magnetostrictive FeCoSiB coated ZnO Microstructures by Bragg Coherent X-Ray Diffraction Imaging
<p>Five sets of raw data from (Fe<sub>90</sub>Co<sub>10</sub>)<sub>78</sub>Si<sub>12</sub>B<sub>10</sub> coated ZnO microstructure (rod) investigated by Bragg coherent X-ray diffraction imaging. FeCoSiB is a magnetostrictive alloy, thus a changing strain is expected for applied magnetic fields.</p> <p>Included is data from the same spatial positions along the c-axis of the ZnO rod at five different magnetic flux densities [0, 4.4, 5.6, 9.1, 13.2]/mT. Futher on called P1 to P5. For each position there is a .nxs file of a rocking scan around the {0001} Bragg reflection, collected by a 2D detector and other recorded values, e.g. motor positions, counter values. </p>
X-ray diffraction images of the beta4 tetramer of the C-terminal peptide of the split chain transketolase
<p>X-ray images for PDB entry 6YAJ</p> <p>DOI for the pdb is https://doi.org/10.2210/pdb6YAJ/pdb</p> <p>Title: A 'Split-Gene' Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans : Structure and Biochemical Characterization.<br> Journal: Front Microbiol<br> Volume: 11<br> Pages: 592353 - 592353<br> Year: 2020<br> PubMed ID: 33193259<br> DOI: 10.33 89/fmicb .2020.592353</p> <p> </p> <p> </p>
X-ray diffraction images of the alpah2beta2 heterotetramer of the split chain transketolase
<p>Data were collected on Diamond I04-1 14 Dec 2013.</p> <p> James, P.,Isupov, M.N.,De Rose, S.A.,Sayer, C.,Cole, I.S.,Littlechild, J.A.<br> <br> A 'Split-Gene' Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans : Structure and Biochemical Characterization.<br> <br> Journal: Front Microbiol<br> Volume: 11<br> Pages: 592353 - 592353<br> Year: 2020<br> PubMed ID : 3319 3259<br> DOI: 10.3389/fmicb.2020.592353<br> <br> PDB DOI: https://doi.org/10.2210/pdb6YAK/pdb</p>
Data from: Visualizing mineralization processes and fossil anatomy using synchronous synchrotron X-ray fluorescence and X-ray diffraction mapping
<p>Fossils, including those that occasionally preserve decay-prone soft-tissues, are mostly made of minerals. Accessing their chemical composition provides unique insight into their past biology and/or the mechanisms by which they preserve, leading to a series of developments in chemical and elemental imaging. However, the mineral composition of fossils, particularly where soft-tissues are preserved, is often only inferred indirectly from elemental data, while X-ray diffraction that specifically provides phase identification received little attention. Here, we show the use of synchrotron radiation to generate not only X-ray fluorescence elemental maps of a fossil, but also mineralogical maps in transmission geometry using a two-dimensional area detector placed behind the fossil. This innovative approach was applied to millimetre-thick cross-sections prepared through three-dimensionally preserved fossils, as well as to compressed fossils. It identifies and maps mineral phases and their distribution at the microscale over centimetre-sized areas, benefitting from the elemental information collected synchronously, and further informs on texture (preferential orientation), crystallites size and local strain. Probing such crystallographic information is instrumental in defining mineralization sequences, reconstructing the fossilization environment and constraining preservation biases. Similarly, this approach could potentially provide new knowledge on other (bio)mineralization processes in environmental sciences. We also illustrate that mineralogical contrasts between fossil tissues and/or the encasing sedimentary matrix can be used to visualize hidden anatomies in fossils.</p>
Simultaneous X-ray diffraction from multiple single crystals of macromolecules
<p>X-ray diffraction datasets from the<br /> publication: K. S. Paithankar, H. O. Sørensen, J. P. Wright, S. Schmidt, H. F. Poulsen and E. F. Garman*</p> <p>Acta Cryst. (2011). D67, 608-618 doi:10.1107/S0907444911015617</p> <p>The potential in macromolecular crystallography for using multiple crystals to collect X-ray diffraction data simultaneously from assemblies of up to seven crystals is explored. The basic features of the algorithms used to extract data and their practical implementation are described. The procedure could be useful both in relation to diffraction data obtained from intergrown crystals and to alleviate the problem of rapid diffraction decay arising from the effects of radiation damage.</p>
Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
<p>These are X-ray diffraction data from the publication<br> Enderle, M.E, McCarthy, A, Paithankar, K. S, and Grininger, M</p> <p>Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I.</p> <p>Acta Crystallogr F Struct Biol Commun. 2015 Nov;71(Pt 11):1401-7</p> <p>CC-BY-SA license</p> <p>MD5SUMS</p> <p>a774aabcd316b5b200ef5c08b109ba9a crystal-form-II_part-1.tar.lzma</p> <p>3596da75621648cc0ac5ee84b26deab0 crystal-form-II_part-2.tar.lzma</p> <p>8a5410ce3178c814d7a127491e68ca0a crystal-form-I_part-1.tar.lzma</p> <p>259614e1b2cfe089141fb7baa846af7e crystal-form-I_part-2.tar.lzma</p>
X-ray diffraction images for DPF3 tandem PHD fingers co-crystallized with an acetylated histone-derived peptide
<p>This submission includes a tar archive of bzipped diffraction images recorded with the ADSC Q315r detector at the Advanced Photon Source of Argonne National Laboratory, Structural Biology Center beam line 19-ID. Relevant meta data can be found in the headers of those diffraction images.</p> <p>Please find below the content of an input file XDS.INP for the program XDS (Kabsch, 2010), which may be used for data reduction. The "NAME_TEMPLATE_OF_DATA_FRAMES=" item inside XDS.INP may need to be edited to point to the location of the downloaded and untarred images.</p> <p>!!! Paste lines below in to a file named XDS.INP</p> <p>DETECTOR=ADSC MINIMUM_VALID_PIXEL_VALUE=1 OVERLOAD= 65000<br /> DIRECTION_OF_DETECTOR_X-AXIS= 1.0 0.0 0.0<br /> DIRECTION_OF_DETECTOR_Y-AXIS= 0.0 1.0 0.0<br /> TRUSTED_REGION=0.0 1.05<br /> MAXIMUM_NUMBER_OF_JOBS=10<br /> ORGX= 1582.82 ORGY= 1485.54<br /> DETECTOR_DISTANCE= 150<br /> ROTATION_AXIS= -1.0 0.0 0.0<br /> OSCILLATION_RANGE=1<br /> X-RAY_WAVELENGTH= 1.2821511<br /> INCIDENT_BEAM_DIRECTION=0.0 0.0 1.0<br /> FRACTION_OF_POLARIZATION=0.90<br /> POLARIZATION_PLANE_NORMAL= 0.0 1.0 0.0<br /> SPACE_GROUP_NUMBER=20<br /> UNIT_CELL_CONSTANTS= 100.030 121.697 56.554 90.000 90.000 90.000<br /> DATA_RANGE=1 180<br /> BACKGROUND_RANGE=1 6<br /> SPOT_RANGE=1 3<br /> SPOT_RANGE=31 33<br /> MAX_CELL_AXIS_ERROR=0.03<br /> MAX_CELL_ANGLE_ERROR=2.0<br /> TEST_RESOLUTION_RANGE=8.0 3.8<br /> MIN_RFL_Rmeas= 50<br /> MAX_FAC_Rmeas=2.0<br /> VALUE_RANGE_FOR_TRUSTED_DETECTOR_PIXELS= 6000 30000<br /> INCLUDE_RESOLUTION_RANGE=50.0 1.7<br /> FRIEDEL'S_LAW= FALSE<br /> STARTING_ANGLE= -100 STARTING_FRAME=1<br /> NAME_TEMPLATE_OF_DATA_FRAMES= ../x247398/t1.0???.img</p> <p>!!! End of XDS.INP</p> <p> </p> <p> </p>
Low dose, high multiplicity thermolysin X-ray diffraction data from Diamond Light Source beamline I03
<p>Low dose, high multiplicity X-ray diffraction data recorded from a thermolysin crystal prepared according to standard protocols as part of ongoing research. The data were recorded with low transmission to ensure minimal radiation damage, with the side-effect that the individual reflections are exceedingly weak even at low resolution, and the majority of background pixels have no counts.</p>
High resolution X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase complexed with levulinic acid.
<p>X-ray diffraction images collected at DESY Hamburg in June 1998 using beamline BW7B. </p>
X-ray diffraction images for endothiapepsin co-crystallised with inhibitor H189 to 0.94 Angstrom resolution.
<p>X-ray diffraction images collected on 23rd May 2000 at the BW7B beamline of DESY (Hamburg). </p>
Single crystal X-ray diffraction data for Hoch_3836 (1-98)
<p>Single crystal X-ray diffraction data for Hoch_3836 (1-987) related to PDBID: 5N5F</p> <p>Data collected at Diamond Light Source, UK.</p>
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International Brain Laboratory public data
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OpenNeuro
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