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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 11 (1991), S. 153-157 
    ISSN: 0887-3585
    Keywords: pyruvate kinase ; crystals ; electron paramagnetic resonance ; oxalate ; pyruvate ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Pyruvate kinase from rabbit muscle has been crystallized in a form suitable for high resolution X-ray analysis. Complexes of the enzyme with Mn2+ and either pyruvate or oxalate crystallize from solutions of polyethyleneglycol 8000 at pH 6.0. Crystals obtained from solutions of the complexes with pyruvate or oxalate appear isomorphous and belong to the triclinic space group P1. The crystals have unit cell dimensions a = 83.3(4) Å, b = 109.4(6) Å, c = 145.7(7) Å, α = 94.9°, β = 93.6°, γ = 112.2°. These crystals diffract to better than 2.4 Å resolution and are stable in the X-ray beam for at least 20 hr. Electron paramagnetic resonance measurements on a single crystal show that Mn2+ is bound to the crystalline protein.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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