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Literature DB >> 23722859

Crystallization of recombinant green mamba ρ-Da1a toxin during a lyophilization procedure and its structure determination.

Arhamatoulaye Maïga¹, Laura Vera, Charles Marchetti, Alain Lorphelin, Laurent Bellanger, Gilles Mourier, Denis Servent, Nicolas Gilles, Enrico Adriano Stura.

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.

Entities: Species

Keywords: lyophilization; three-finger fold toxin; weak data

Mesh：

Substances：

Year: 2013 PMID： 23722859 PMCID： PMC3668600 DOI： 10.1107/S1744309113011470

Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091

21 in total

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3 in total