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  • Title: Crystallization and preliminary X-ray diffraction studies of peroxidase from a fungus Arthromyces ramosus.
    Author: Kunishima N, Fukuyama K, Wakabayashi S, Sumida M, Takaya M, Shibano Y, Amachi T, Matsubara H.
    Journal: Proteins; 1993 Feb; 15(2):216-20. PubMed ID: 8382820.
    Abstract:
    Peroxidase (donor: H2O2 oxidoreductase [EC 1.11.1.7]) was purified from the culture broth of the hyphomycete Arthromyces ramosus in the early log phase to show a single band on SDS-PAGE. The crystals of A. ramosus peroxidase (ARP) were formed by salting out with ammonium sulfate at room temperature and pH 7.5. The repeated seeding technique was employed to grow the crystals to the size large enough for X-ray diffraction study. The crystals were characterized as tetragonal, space group P4(2)2(1)2, with unit cell dimensions of a = b = 74.5 A, c = 117.6 A. The asymmetric unit contains one molecule of peroxidase. They diffract X-rays to at least 2.0 A resolution and are stable to X-rays.
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