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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization of recombinant green mamba rho-Da1a toxin during a lyophilization procedure and its structure determination
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Crystallization of recombinant green mamba rho-Da1a toxin during a lyophilization procedure and its structure determination

机译：冻干过程中重组绿色曼巴rho-Da1a毒素的结晶及其结构测定

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摘要

rho-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 alpha(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 angstrom, and diffracted to 1.95 angstrom resolution. The structure solved by molecular replacement showed strong similarities to green mamba muscarinic toxins.
机译：来自东部绿曼巴蛇（Dendroaspis angusticeps）毒液的rho-Da1a毒素是一种具有65个氨基酸的多肽，对G蛋白偶联的alpha（1A）-肾上腺素受体具有很强的亲和力。这种神经毒素已从再溶解的冻干粉末中结晶出来，但是最好的晶体在冻干过程中会自发生长。晶体属于三角空间群P3（1）21，单位晶胞参数a = b = 37.37，c = 66.05埃，并衍射至1.95埃分辨率。通过分子置换解决的结构显示出与绿曼巴毒蕈碱毒素的强相似性。

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