Crystallization and preliminary X-ray analysis of an intact soluble-form variant surface glycoprotein from the African trypanosome, Trypanosoma brucei.
Crystallization and preliminary X-ray analysis of an intact soluble-form variant surface glycoprotein from the African trypanosome, Trypanosoma brucei.
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来自非洲锥虫布氏锥虫的完整可溶形式变异表面糖蛋白的结晶和初步 X 射线分析。
DOI：
10.1016/0022-2836(91)90254-4
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发表时间：
1991
影响因子：
5.6
通讯作者：
Wiley,DC
中科院分区：
文献类型：
--
作者：
Down,JA;Garman,SC;Gurnett,AM;Turner,MJ;Wiley,DC
从布氏锥虫（Trypanosomabrucei）中获得了完整的变异表面糖蛋白（VSG）ILTat 1.24。包含三分之二序列的蛋白质的氨基末端结构域先前在蛋白水解消化后结晶。现在，完整的VSG晶体已从50 m m-Mes（pH 6.5）含有62%（w-v）饱和硫酸铵生长。通过hplc凝胶过滤和与VSG羧基末端磷酸肌醇寡糖抗体反应，证明晶体含有完整的VSG。晶体空间群为P6 2 2 2（或P6 4 2 2），晶胞尺寸a= 6= 184 A <$，c= 2 14 A <$。结晶等电聚焦可能促进了结晶。
The intact variant surface glycoprotein (VSG) ILTat 1.24 from Trypanosoma brucei has been crystallized. An amino-terminal domain of the protein comprising two thirds of the sequence had been crystallized previously after proteolytic digestion. Now intact VSG crystals have been grown from 50 m m-Mes (pH 6.5) containing 62%(w v) saturated ammonium sulfate. The crystals are demonstrated to contain the intact VSG by hplc gel filtration and reaction with an antibody to the inositol phosphate oligosaccharide on the VSG carboxy terminus. The space group of the crystals is P6 2 22 (or P6 4 22) with unit cell dimensions a= 6= 184 A ̊ and c= 214 A ̊. Preparative isoelectric focusing may have facilitated crystallization.