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

ABSTRACT: ?-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 ?(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.

SUBMITTER: Maiga A

PROVIDER: S-EPMC3668600 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature

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

Maïga Arhamatoulaye A Vera Laura L Marchetti Charles C Lorphelin Alain A Bellanger Laurent L Mourier Gilles G Servent Denis D Gilles Nicolas N Stura Enrico Adriano EA

Acta crystallographica. Section F, Structural biology and crystallization communications 20130529 Pt 6

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 r ...[more]

PMID: 23722859

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