biostudies-literatureUnknown69(Pt 6)Maiga Aρ-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.Acta crystallographica. Section F, Structural biology and crystallization communications704-9https://www.ebi.ac.uk/biostudies/studies/S-EPMC3668600biostudies-literatureCrystallization of recombinant green mamba ρ-Da1a toxin during a lyophilization procedure and its structure determination.PMC3668600Gilles NServent DStura EALorphelin ABellanger LMaiga AMourier GVera LMarchetti CfalseCrystallization of recombinant green mamba ρ-Da1a toxin during a lyophilization procedure and its structure determination.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.2013-01-01T00:00:00Z2013 Jun2025-04-19T14:57:12.694Z2019-03-27T01:10:39ZS-EPMC36686002372285910.1107/S174430911301147010.1107/s1744309113011470