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  • International Union of Crystallography (IUCr)  (2)
  • 1995-1999  (2)
  • 1965-1969
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  • 1
    Electronic Resource
    Electronic Resource
    Ribonuclease from Streptomyces aureofaciens at Atomic Resolution (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 327-344 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of ribonuclease from Streptomyces aureofaciens diffract to atomic resolution at room temperature. Using synchrotron radiation and an imaging-plate scanner, X-ray data have been recorded to 1.20 Å resolution from a crystal of native enzyme and to 1.15 Å from a crystal of a complex with guanosine-2′-monophosphate. Refinement with anisotropic atomic temperature factors resulted in increased accuracy of the structure. The R factors for the two structures are 10.6 and 10.9%. The estimated r.m.s. error in the coordinates is 0.05 Å, less than half that obtained in the previous analysis at 1.7 Å resolution. For the well ordered part of the main chain the error falls to below 0.02 Å as estimated from inversion of the least-squares matrix. The two independent molecules in the asymmetric unit allowed detailed analysis of peptide planarity and some torsion angles. The high accuracy of the analysis revealed density for a partially occupied anion in the nucleotide binding site of molecule A in the native structure which was not seen at lower resolution. The anisotropic model allowed correction of the identity of the residue at position 72 from cysteine to threonine. Cys72 SG had been modelled in previous analyses with two conformations. The solvent structure was modelled by means of an automated procedure employing a set of objective criteria. The solvent structure for models refined using different programs with isotropic and anisotropic description of thermal motion is compared.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995007669
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of the Saccharomycopsis fibuligera glucoamylase expressed from the GLU1 gene in Escherichia coli (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 782-783 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The active non-glycosylated glucoamylase, overexpressed from the Saccharomycopsis fibuligera GLU1 gene in Escherichia coli BL21(DE3), has been purified from the solubilized inclusion bodies and then renatured in vitro. Crystals of the recombinant glucoamylase were obtained by vapour diffusion using PEG as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell dimensions of a = 58.1, b = 87.8 and c = 99.9 Å, and diffract to 1.7 Å resolution. This is the first report of the crystallization of the full-length glucoamylase corresponding to the mature enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997006835
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    Paper (German National Licenses)
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