Preliminary crystallographic study of peanut peroxidase | Zendy

Ban N. | Zendy; Van Huystee R. B. | Zendy; Day J. | Zendy; Greenwood A. | Zendy; Larson S. | Zendy; Esnault R. | Zendy; McPherson A. | Zendy

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Preliminary crystallographic study of peanut peroxidase

Author(s) -

Ban N.,

Van Huystee R. B.,

Day J.,

Greenwood A.,

Larson S.,

Esnault R.,

McPherson A.

Publication year - 1992

Publication title -

acta crystallographica section b

Language(s) - English

Resource type - Journals

eISSN - 1600-5740

pISSN - 0108-7681

DOI - 10.1107/s0108768191008807

Subject(s) - orthorhombic crystal system , crystallography , peroxidase , resolution (logic) , glycoprotein , covalent bond , molecule , chemistry , cationic polymerization , crystallization , materials science , crystal structure , biochemistry , enzyme , organic chemistry , artificial intelligence , computer science

The cationic isozyme of peroxidase isolated from suspension cultures of peanut cells is a heme-containing and calcium-dependent glycoprotein having four covalently attached oligosaccharide chains. Attempts were made to crystallize the glycoprotein for X-ray diffraction analysis, and these have met with some success. Crystals have now been grown that are suitable for a full three-dimensional structural analysis. The crystals are thin plates and we have shown them to be of the orthorhombic space group P2(1)2(1)2(1) with a = 48.1, b = 97.2, c = 146.2 A. The crystals diffract to beyond 2.8 A resolution, appear to be stable to lengthy X-ray exposure, and contain two molecules of 40,000 daltons each in the asymmetric unit.

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