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  • 1
    Electronic Resource
    Electronic Resource
    Preparation and crystallization of a Bacillus subtilis arsenate reductase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1718-1721 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Arsenate reductase (AR) in B. subtilis is encoded by the chromosomal arsC gene. Together with arsB and arsR, arsC participates in detoxification processes for the arsenate and arsenite ions. Full-length arsenate reductase without any modification has been expressed in Escherichia coli and purified in a soluble form. The recombinant protein has been crystallized at 277 K using polyethyleneglycol (PEG) or poly(ethyleneglycol) methyl ether (PME) as the main precipitant. At least two forms of crystals large enough for data collection have been obtained from wild-type protein under different conditions. An orthorhombic crystal diffracted to beyond 2.2 Å with space group P212121 and unit-cell parameters a = 51.22, b = 91.62, c = 101.93 Å. A near-complete data set has been collected to 2.5 Å. The application of the flash-annealing technique was crucial for high resolution during the data collection. The SeMet-substituted AR has also been produced and crystallized under very similar conditions as the wild type, but the unit-cell parameters are very different. The crystals of the SeMet protein diffracted to higher resolution than those of the wild type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901014020
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary X-ray analysis of a maize cytokinin glucoside specific β-glucosidase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 140-142 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Zm-p60.1, a cytokinin glucoside specific β-glucosidase from maize, is a key enzyme involved in plant development and growth. It has been overexpressed in soluble form from Escherichia coli with a His tag at its N-terminus. The recombinant protein has been purified and crystallized at room temperature using PEG 4000 as the main precipitant. At least three crystal forms have been observed from very similar growth conditions. A flash-annealed monoclinic crystal diffracted to high resolution (beyond 2 Å) with space group P21 and unit-cell parameters a = 55.66, b = 110.72, c = 72.94 Å, β = 92.10°. The asymmetric unit is estimated and confirmed by molecular-replacement solution to contain one Zm-p60.1 dimer, giving a crystal volume per protein mass (VM) of 1.89 Å3 Da−1 and a solvent content of 35%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900014001
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (1994)
    [s.l.] : Nature Publishing Group
    Nature 370 (1994), S. 575-578 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The bovine liver low-molecular-weight PTPase contains 157 amino-acid residues (Mr 17,953)2; it has been crystallized in 0.1 M acetate buffer, pH 5.5, in the presence of 40% saturated ammonium sulphate10. The structure of the enzyme was solved using the multiple isomorphous replacement method ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/370575a0
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    Paper (German National Licenses)
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