Crystallization and preliminary X-ray study of the common edible mushroom (Agaricus bisporus) lectin

CARRIZO ME; IRAZOQUI FJ; LARDONE RD; NORES GA; CURTINO JA; CAPALDI S; PERDUCA M; MONACO HL

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Año: 2004 vol. 60 p. 718 - 718

0907-4449

font face="Advt93-r" size="1"> The lectin from the common edible mushroom Agaricus bisporus (ABL) belongs to the group of proteins that have the property of binding the Thomsen±Friedenreich antigen (T-antigen) selectively and with high afÆnity, but does not show any sequence similarity to the other proteins that share this property. The ABL sequence is instead similar to those of members of the saline-soluble fungal lectins, a protein family with pesticidal properties. The presence of different isoforms has been reported. It has been found that in order to be able to grow diffraction-quality crystals of the lectin, it is essential to separate the isoforms, which was performed by preparative isoelectric focusing. Using standard procedures, it waspossible to crystallize the most basic of the forms by either vapour diffusion or equilibrium dialysis, but attempts to grow crystals of theother more acidic