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  • 1
    Electronic Resource
    Electronic Resource
    Laue crystallography: coming of age (1999)
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 6 (1999), S. 891-917 
    Details
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A renewed interest in the Laue diffraction technique has been brought about by the development of new, more intense and brilliant synchrotron sources along with their insertion devices such as wigglers and undulators, and by the prospect of using these sources to study structural dynamics by time-resolved crystallography. Theoretical studies during the past decade have identified unique features of the polychromatic diffraction geometry and greatly improved our understanding of the Laue method. This led to innovative approaches to Laue data processing and its software implementation. Most of the problems in Laue data processing, considered for a long time to limit the applicability of the technique, have been solved. Significant advances have also been made in the development of synchrotron sources, beamline optics and instrumentation, and the X-ray detectors. Static Laue experiments yield structure amplitudes that equal those from monochromatic data in quality. When coupled with careful consideration of data-collection strategies and reaction initiation in crystals, a series of successful time-resolved Laue experiments on biological systems have been conducted. These have revealed information on structural dynamics inaccessible to any other conventional diffraction method. These static and time-resolved experiments demonstrate that the Laue method is coming of age. They also suggest avenues for future improvements: a correct treatment of finite mosaic spread and the associated energy width of Laue spots; consideration of diffuse scattering; and determination of intermediate structures in time-resolved experiments in which those intermediates do not attain a high concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0909049599006366
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning, sequence and crystallographic structure of recombinant iron superoxide dismutase from Pseudomonas ovalis (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1359-1366 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The gene encoding the iron-dependent superoxide dismutase from Pseudomonas ovalis was cloned from a genomic library and sequenced. The ORF differs from the previously published protein sequence, which was used for the original structure determination, at 16 positions. The differences include three additional inserted residues, one deleted residue and 12 point substitutions. The gene was subcloned and the recombinant protein overexpressed, purified and crystallized in a trigonal space group. The structure was determined by molecular replacement and was refined to 2.1 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900009537
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of bacterial cytosine deaminase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1643-1645 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Cytosine deaminase (CD) is found in prokaryotes and fungi (but not higher eukaryotes) and catalyzes the deamination of cytosine and 5-fluorocytosine to uracil and 5-fluorouracil, respectively. The former activity is an important function within the pyrimidine-salvage pathway, while the latter activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. Recombinant bacterial CD from Escherichia coli has been subcloned, overexpressed, purified and crystallized for structural analysis. The crystals belong to space group R32, with unit-cell parameters a = b = 109.1, c = 240 Å and diffract to at least 1.5 Å resolution at a synchrotron X-ray source. There is one enzyme subunit per asymmetric unit and the Matthews coefficient VM is 2.8 Å3 Da−1, corresponding to a solvent content of 56%. Selenomethionine-containing protein has been prepared and crystallized for MAD phasing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901011064
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