Preliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micado

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, s uch as mast cell degranulation, hemolytic activity and also reveals antimic robial activity. A mastoparan toxin isolated from the venom of Anterhynchiu m flavomarginatum micado has been crystallized. At room temperature these c rystals diffracted to 2.8 Angstrom resolution. However, upon cooling to cry ogenic temperature around 85 K, the original resolution limit could be impr oved to 2.0 Angstrom. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation. (C) 3001 Elsevier Science B.V. All rights reserved.