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Crystallization of recombinant green mamba ρ-Da1a toxin during a lyophilization procedure and its structure
Arhamatoulaye Maïga1, Laura Vera, Charles Marchetti
1CEA, DSV, iBiTec-S, Service d'Ingénierie Moléculaire des Protéines, 91191 Gif-sur-Yvette, France.
Abstract:
ρ-Da1a toxin from eastern green mamba (Dendroaspis angusticeps) venom is a polypeptide of 65 amino acids with a strong affinity for the G-protein-coupled α(1A)-adrenoceptor. This neurotoxin has been crystallized from resolubilized lyophilized powder, but the best crystals grew spontaneously during lyophilization. The crystals belonged to the trigonal space group P3(1)21, with unit-cell parameters a = b = 37.37, c = 66.05 Å, and diffracted to 1.95 Å resolution. The structure solved by molecular replacement showed strong similarities to green mamba muscarinic toxins.
