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  • International Union of Crystallography  (3)
  • 1
    In: Acta Crystallographica Section D, November 2004, Vol.60(11), pp.2019-2021
    Description: Regucalcin is a novel calcium ion (Ca) binding protein that does not contain an EF‐hand motif as a Ca‐binding domain and has been demonstrated to play a multi‐functional role in many cell types. Human liver regucalcin, consisting of 299 amino‐acid residues, was overexpressed in , purified and crystallized by the vapour‐diffusion method in the presence of polyethylene glycol 4000 as a precipitant. A native crystal diffracted to 2.8 Å with synchrotron radiation and belongs to space group 2, with unit‐cell parameters  = 64.87, = 52.52, = 86.38 Å, β = 99.86°. Two molecules most probably exist in the asymmetric unit, corresponding to = 2.2 Å Da. Heavy‐atom derivative data were collected and the Pb derivative showed one high‐occupancy site per molecule.
    Keywords: Regucalcin ; Calcium‐Binding Proteins.
    ISSN: 0907-4449
    E-ISSN: 1399-0047
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  • 2
    In: Acta Crystallographica Section D, October 2003, Vol.59(10), pp.1840-1842
    Description: An ADP‐ribose pyrophosphatase from HB8 was overproduced in and purified. Gel‐filtration chromatography showed the protein to be in a dimeric state. This protein catalyses the Mg‐ or Zn‐dependent hydrolysis of ADP‐ribose to AMP and ribose‐5′‐phosphate. It was crystallized in the absence and the presence of ADP‐ribose by the hanging‐drop vapour‐diffusion method. Complete data sets were collected to 1.50 Å resolution from the apo form using synchrotron radiation and to 2.0 Å resolution from the complexed form. Both crystals belong to space group 321 or 321 and contain one molecule in the asymmetric unit.
    Keywords: Adp‐Ribose ; Adp‐Ribose Pyrophosphatase ; Nudix Hydrolases ; Extreme Thermophile ; Hb8.
    ISSN: 0907-4449
    E-ISSN: 1399-0047
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  • 3
    In: Acta Crystallographica Section D, 01 March 1999, Vol.55(3), pp.704-705
    Description: A DNA excision repair enzyme, UvrB, from HB8 was crystallized by the vapor‐diffusion method using lithium sulfate as the precipitant and β‐octylglucoside as an additive. The crystals belong to the trigonal space group 321 or 321, with unit‐cell dimensions of = = 136.0 and = 108.1 Å. The crystal is most likely to contain one UvrB protein in an asymmetric unit with the value of 3.8 Å Da. The crystals diffracted X‐rays beyond 2.9 Å resolution. Although the crystals were sensitive to X‐ray irradiation at room temperature, the frozen crystals at 100 K showed no apparent decay during the intensity measurement.
    Keywords: Nucleic Acids ; Dna Repair ; Uvrb.
    ISSN: 0907-4449
    E-ISSN: 1399-0047
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