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Title
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Crystallization and preliminary X-ray diffraction studies of peroxidase from a fungus Arthromyces ramosus.
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Authors
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N.Kunishima,
K.Fukuyama,
S.Wakabayashi,
M.Sumida,
M.Takaya,
Y.Shibano,
T.Amachi,
H.Matsubara.
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Ref.
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Proteins, 1993,
15,
216-220.
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PubMed id
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Abstract
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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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