Endo-polygalacturonases catalyze the fragmentation and solubilization of the homogalacturonan of the plant cell wan. These enzymes are extracellularly targeted glycoproteins produced by a number of organisms such as fungi, bacteria and plants, and are involved in both pathological and physiological processes. Single crystals of the endopolygalacturonase from the phytopathogenic fungus Fusarium moniliforme were obtained by the vapour-diffusion method at 294 K. The starting material as well as the crystal consist of three forms with different degrees of glycosylation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) and diffract to 1.9 Angstrom resolution on a synchrotron-radiation source under cryocooling conditions.

Crystallization and preliminary X-ray diffraction study of the endo-polygalacturonase from Fusarium moniliforme

CAPRARI, Claudio;
1999

Abstract

Endo-polygalacturonases catalyze the fragmentation and solubilization of the homogalacturonan of the plant cell wan. These enzymes are extracellularly targeted glycoproteins produced by a number of organisms such as fungi, bacteria and plants, and are involved in both pathological and physiological processes. Single crystals of the endopolygalacturonase from the phytopathogenic fungus Fusarium moniliforme were obtained by the vapour-diffusion method at 294 K. The starting material as well as the crystal consist of three forms with different degrees of glycosylation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) and diffract to 1.9 Angstrom resolution on a synchrotron-radiation source under cryocooling conditions.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11695/6929
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