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  • American Society of Hematology  (4)
  • International Union of Crystallography (IUCr)  (3)
  • 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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  • 4
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    Hemophilic factor VIII C1- and C2-domain missense mutations and their modeling to the 1.5-angstrom human C2-domain crystal structure (2000)
    American Society of Hematology
    Details
    Publication Date: 2000-08-01
    Description: Factor VIII C domains contain key binding sites for von Willebrand factor (vWF) and phospholipid membranes. Hemophilic patients were screened for factor VIII C-domain mutations to provide a well-characterized series. Mutated residues were localized to the high-resolution C2 structure and to a homology model of C1. Of 30 families found with mutations in the C domains, there were 14 missense changes, and 9 of these were novel. Of the missense mutations, 10 were associated with reduced vWF binding and 8 were at residues with surface-exposed side chains. Six of the 10 mutants had nearly equivalent factor VIII clotting activity and antigen level, suggesting that reduced vWF binding could cause hemophilia by reducing factor VIII stability in circulation. When the present series was combined with previously described mutations from an online international database, 11 C1 and C2 mutations in patients with mild or moderately severe hemophilia A were associated with antibody-inhibitor development in at least one affected individual. Of these substitutions, 6 occurred at surface-exposed residues. As further details of the C1 structure and its interface with C2 become available, and as binding studies are performed on the plasma of more patients with hemophilic C-domain mutations, prediction of surface binding sites should improve, allowing confirmation by site-specific mutagenesis of surface-exposed residues.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 5
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    Hemophilic factor VIII C1- and C2-domain missense mutations and their modeling to the 1.5-angstrom human C2-domain crystal structure (2000)
    American Society of Hematology
    Details
    Publication Date: 2000-08-01
    Description: Factor VIII C domains contain key binding sites for von Willebrand factor (vWF) and phospholipid membranes. Hemophilic patients were screened for factor VIII C-domain mutations to provide a well-characterized series. Mutated residues were localized to the high-resolution C2 structure and to a homology model of C1. Of 30 families found with mutations in the C domains, there were 14 missense changes, and 9 of these were novel. Of the missense mutations, 10 were associated with reduced vWF binding and 8 were at residues with surface-exposed side chains. Six of the 10 mutants had nearly equivalent factor VIII clotting activity and antigen level, suggesting that reduced vWF binding could cause hemophilia by reducing factor VIII stability in circulation. When the present series was combined with previously described mutations from an online international database, 11 C1 and C2 mutations in patients with mild or moderately severe hemophilia A were associated with antibody-inhibitor development in at least one affected individual. Of these substitutions, 6 occurred at surface-exposed residues. As further details of the C1 structure and its interface with C2 become available, and as binding studies are performed on the plasma of more patients with hemophilic C-domain mutations, prediction of surface binding sites should improve, allowing confirmation by site-specific mutagenesis of surface-exposed residues.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 6
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    Structure of a factor VIII C2 domain–immunoglobulin G4κ Fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII (2001)
    American Society of Hematology
    Details
    Publication Date: 2001-07-01
    Description: The development of an immune response to infused factor VIII is a complication affecting many patients with hemophilia A. Inhibitor antibodies bind to antigenic determinants on the factor VIII molecule and block its procoagulant activity. A patient-derived inhibitory immunoglobulin G4κ antibody (BO2C11) produced by an immortalized memory B-lymphocyte cell line interferes with the binding of factor VIII to phospholipid surfaces and to von Willebrand factor. The structure of a Fab fragment derived from this antibody complexed with the factor VIII C2 domain was determined at 2.0 Å resolution. The Fab interacts with solvent-exposed basic and hydrophobic side chains that form a membrane-association surface of factor VIII. This atomic resolution structure suggests a variety of amino acid substitutions in the C2 domain of factor VIII that might prevent the binding of anti-C2 inhibitor antibodies without significantly compromising the procoagulant functions of factor VIII.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 7
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    The tertiary structure and domain organization of coagulation factor VIII (2008)
    American Society of Hematology
    Details
    Publication Date: 2008-02-01
    Description: Factor VIII (fVIII) is a serum protein in the coagulation cascade that nucleates the assembly of a membrane-bound protease complex on the surface of activated platelets at the site of a vascular injury. Hemophilia A is caused by a variety of mutations in the factor VIII gene and typically requires replacement therapy with purified protein. We have determined the structure of a fully active, recombinant form of factor VIII (r-fVIII), which consists of a heterodimer of peptides, respectively containing the A1-A2 and A3-C1-C2 domains. The structure permits unambiguous modeling of the relative orientations of the 5 domains of r-fVIII. Comparison of the structures of fVIII, fV, and ceruloplasmin indicates that the location of bound metal ions and of glycosylation, both of which are critical for domain stabilization and association, overlap at some positions but have diverged at others.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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