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  • International Union of Crystallography (IUCr)  (6)
  • American Geophysical Union (AGU)
  • 2000-2004  (6)
  • 2001  (6)
  • 1
    Digitale Medien
    Digitale Medien
    Characterization of H defects in the aluminium–hydrogen system using small-angle scattering techniques (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 34 (2001), S. 119-129 
    Details
    ISSN: 1600-5767
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Geologie und Paläontologie , Physik
    Notizen: Aluminium foils (99.99% purity) and single crystals (99.999% purity) were charged with hydrogen using a gas plasma method and electrochemical methods, resulting in the introduction of a large amount of hydrogen. X-ray diffraction measurements indicated that within experimental error there was a zero change in lattice parameter after plasma charging. This result is contradictory to almost all other face-centred cubic (f.c.c.) materials, which exhibit a lattice expansion when the hydrogen enters the lattice interstitially. It is hypothesized that the hydrogen does not enter the lattice as an interstitial solute, but instead forms an H–vacancy complex at the surface that diffuses into the volume and then clusters to form H2 bubbles. Small- and ultra-small-angle neutron scattering (SANS, USANS) and small-angle X-ray scattering (SAXS) were primarily employed to study the nature and agglomeration of the H–vacancy complexes in the Al–H system. The SAXS results were ambiguous owing to double Bragg scattering, but the SANS and USANS investigation, coupled with results from inelastic neutron scattering, and transmission and scanning electron microscopy, revealed the existence of a large size distribution of hydrogen bubbles on the surface and in the bulk of the Al–H system. The relative change in lattice parameter is calculated from the pressure in a bubble of average volume and is compared with the experimentally determined value.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0021889800018239
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Location of Zn within the Mg12(LaxCe1−x) lattice by X-ray incoherent channelling patterns (2001)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 321-332 
    Details
    ISSN: 1600-5724
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: Systematic electron diffraction studies on intermetallic precipitates formed within a lightweight Mg–RE–Zn alloy (RE = La or Ce) identify these to be of structural type Mn12Th (space group I4/mmm). Analytical electron microscopy yields an overall composition of Mg12(LaxCe1−x) with x ̃0.43, with 1 at.% Zn incorporated within the lattice. Variations in characteristic X-ray emission rates, as an electron beam is rocked near zone-axis orientations, are used to form two-dimensional channelling patterns, termed X-ray incoherent channelling patterns. This channelling contrast enables a specific sublattice site that is occupied by Zn to be unambiguously identified within the Mg12RE lattice. The particular sublattice site is denoted by the Wyckoff letter f, and is one of the three different Mg sublattice sites f, i and j. Of these three sites, the Wigner–Seitz cell that is centred on the f sublattice site has the largest Mg–RE interatomic distance, and therefore the f site is expected to be favoured for accommodating the substitution of a larger Zn atom.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0108767300019577
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    The structure and domain organization of Escherichia coli isocitrate lyase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1209-1218 
    Details
    ISSN: 1399-0047
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 Å resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0907444901008642
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    X-LIGAND: an application for the automated addition of flexible ligands into electron density (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 696-705 
    Details
    ISSN: 1399-0047
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: With the advent of drug-design experiments where the interaction between a protein and a ligand is determined using X-ray crystallography, the use of automated methods for modelling the ligand into electron density represents a powerful tool. Once the protein structure has been determined by crystallography it is normal that subsequent ligand-complex structures are isomorphous, or nearly so, with the original structure and it is necessary only to determine the fit of ligand to any unsatisfied electron density. The X-LIGAND application was designed with this protocol in mind and provides a tool that searches for unsatisfied electron density and then fits flexible ligands to this within minutes without user intervention.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0907444901003894
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Creating structure features by data mining the PDB to use as molecular-replacement models (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1421-1427 
    Details
    ISSN: 1399-0047
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: Mathematical data-mining techniques to generate a representative set of protein fragments are described. Protein fragments are used as search models within the macromolecular phasing method of molecular replacement to attempt to phase protein data without a homologous model correctly. Preliminary investigations using these fragments indicate that molecular replacement with AMoRe is not sensitive enough to phase myoglobin or insulin data sufficiently for successful refinement. The results suggest that more advanced molecular replacement techniques may be successful, though at present these are not computationally practical.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0907444901012483
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata) (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 451-453 
    Details
    ISSN: 1399-0047
    Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik
    Notizen: Glycerol-3-phosphate 1-acyltransferase (E.C. 2.3.1.15; G3PAT) catalyses the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acylCoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol 3-phosphate. Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. These crystals are most likely to belong to space group P212121, with approximate unit-cell parameters a = 61.1, b = 65.1, c = 103.3 Å, α = β = γ = 90° and a monomer in the asymmetric unit. X-ray diffraction data to 1.9 Å resolution have been collected in-house using a MAR 345 imaging-plate system.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1107/S0907444901000257
    Standort Signatur Erwartet Verfügbarkeit
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