Overexpression in Pichia pastoris and Crystallization of an Elicitor Protein Secreted by the Phytopathogenic Fungus, Phytophthora cryptogea - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Protein Expression and Purification Année : 1996

Overexpression in Pichia pastoris and Crystallization of an Elicitor Protein Secreted by the Phytopathogenic Fungus, Phytophthora cryptogea

Résumé

A synthetic gene encoding β-cryptogein, a member of the elicitin family, has been cloned into a vector for expression by the methylotrophic yeast,Pichia pastoris.Having first optimized the gene construction for secretion, we have overexpressed a modified β-cryptogein in a secreted form. A purification scheme suited to this expression system has been developed and highly pure, biologically active protein has been obtained. For structural analysis of this recombinant β-cryptogein, and new mutated forms thereof, optimal conditions for the crystallization of this protein have been determined and crystals that diffract to 2.2 Å have been obtained.

Dates et versions

hal-02906918 , version 1 (28-07-2020)

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Michael O'Donohue, Guillaume Boissy, Jean-Claude Huet, Claude Nespoulous, Simone Brunie, et al.. Overexpression in Pichia pastoris and Crystallization of an Elicitor Protein Secreted by the Phytopathogenic Fungus, Phytophthora cryptogea. Protein Expression and Purification, 1996, 8 (2), pp.254-261. ⟨10.1006/prep.1996.0098⟩. ⟨hal-02906918⟩

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