| Autor: |
O'Donohue, Michael J., Boissy, Guillaume, Huet, Jean-Claude, Nespoulous, Claude, Brunie, Simone, Pernollet, Jean-Claude |
| Zdroj: |
Protein Expression and Purification; September 1996, Vol. 8 Issue: 2 p254-261, 8p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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