Expression, purification, crystallization and preliminary X-ray diffraction analysis of alpha-11 giardin from Giardia lamblia.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of alpha-11 giardin from Giardia lamblia.
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DOI：
10.1107/s1744309106039650
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发表时间：
2006-11
期刊：
影响因子：
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通讯作者：
P. Pathuri;E. Nguyen;H. Luecke
中科院分区：
文献类型：
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作者：
P. Pathuri;E. Nguyen;H. Luecke
α-11贾第虫蛋白是一种来自膜联蛋白超家族的蛋白质，是一种来自肠道原生动物寄生虫贾第虫的35.0 kDa蛋白质，其引发一种称为贾第虫病的腹泻形式。在这里，克隆，表达，纯化和结晶的α-11贾第素在两种不同的条件下，在两个不同的空间群的报告。来自第一条件的晶体衍射到1.1 A并且属于原始正交空间群，而来自第二条件的晶体（其在结晶溶液中包括钙）衍射到2.93 A并且属于原始单斜空间群。确定α-11贾第虫素的详细原子结构将更好地了解其生物学功能，并可能确定这类蛋白质是否是对抗贾第虫病的潜在药物靶点。
Alpha-11 Giardin, a protein from the annexin superfamily, is a 35.0 kDa protein from the intestinal protozoan parasite Giardia lamblia which triggers a form of diarrhea called giardiasis. Here, the cloning, expression, purification and the crystallization of alpha-11 giardin under two different conditions and in two different space groups is reported. Crystals from the first condition diffracted to 1.1 A and belong to a primitive orthorhombic space group, while crystals from the second condition, which included calcium in the crystallization solution, diffracted to 2.93 A and belong to a primitive monoclinic space group. Determination of the detailed atomic structure of alpha-11 giardin will provide a better insight into its biological function and might establish whether this class of proteins is a potential drug target against giardiasis.