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Crystallization and preliminary X‐ray diffraction studies of peroxidase from a fungus Arthromyces ramosus
Author(s) -
Kunishima Naoki,
Fukuyama Keiichi,
Wakabayashi Sadao,
Sumida Motoo,
Takaya Masamitsu,
Shibano Yuji,
Amachi Teruo,
Matsubara Hiroshi
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340150213
Subject(s) - ammonium sulfate , peroxidase , tetragonal crystal system , crystallography , crystallization , oxidoreductase , diffraction , resolution (logic) , chemistry , x ray crystallography , x ray , phase (matter) , materials science , enzyme , crystal structure , optics , physics , chromatography , biochemistry , organic chemistry , artificial intelligence , computer science
Peroxidase (donor: H 2 O 2 oxi‐doreductase [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 P 4 2 2 1 2, with unit cell dimensions of a = b = 74.5 Å, c = 117.6 Å. The asymmetric unit contains one molecule of peroxidase. They diffract X‐rays to at least 2.0 Å resolution and are stable to X‐rays. © 1993 Wiley‐Liss, Inc.