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  • International Union of Crystallography (IUCr)  (2)
  • 1995-1999  (2)
  • 1950-1954
  • 1935-1939
  • 1996  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Refinement and structural analysis of bovine cytochrome b5 at 1.5 Å Resolution (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 65-76 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of bovine liver cytochrome b5, a soluble 93-residue proteolytic fragment of a 16 kDa membrane-bound hemoprotein, initially solved at 2.0 Å resolution, has been refined at 1.5 Å using data collected on a diffractometer. Refinement to 2.0 Å resolution used the Hendrickson-Konnert procedure PROLSQ and was then extended to 1.5 Å resolution using the program PROFFT. Only residues 3–87 could be identified in the model and these residues together with 93 water molecules gave an agreement factor of R = 0.161 for data in the resolution range 1.5–5 Å. The structure was finally refined using the program X-PLOR, which enabled alternate conformers to be modelled for several surface side chains. Residues 1 and 2 at the amino terminus of the protein and residue 88 near the carboxyl terminus could be identified from these electron-density maps. However the remaining disordered carboxy-terminal residues could not successfully be included in the model. A total of 117 solvent molecules were included in the final refinement to give R = 0.164 for the data between 1.5 and 10 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995007827
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  • 2
    Electronic Resource
    Electronic Resource
    X-ray Structure of the Cupredoxin Amicyanin, from Paracoccus denitrificans, Refined at 1.31 Å Resolution (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 676-686 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: High-resolution X-ray diffraction data to dmin = 1.31 Å were collected on a Xuong-Hamlin area detector from crystals of the blue-copper protein amicyanin, isolated from P. denitrificans. With coordinates from the earlier 2.0 Å structure determination as a starting point, simulated annealing and restrained positional and temperature factor refinements using the program X-PLOR resulted in a final R factor of 15.5%, based on 21 131 unique reflections in the range 8.0–1.3 Å. Comparison of the 1.31 Å structure with that at 2.0 Å shows the same basic features. However, the high-resolution electron-density maps clearly reveal additional solvent molecules and significant discrete disorder in protein side chains and within the solvent structure. As a consequence of modelling side-chain disorder, several new hydrogen-bonding interactions were identified.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996001072
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    Paper (German National Licenses)
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