Pathuri Puja, Nguyen Emily Tam, Luecke Hartmut
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1108-12. doi: 10.1107/S1744309106039650. Epub 2006 Oct 20.
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.
α-11贾第素是膜联蛋白超家族的一种蛋白质,是来自肠道原生动物寄生虫蓝氏贾第鞭毛虫的一种35.0 kDa蛋白质,它会引发一种名为贾第虫病的腹泻。本文报道了α-11贾第素在两种不同条件下、两种不同空间群中的克隆、表达、纯化及结晶情况。第一种条件下得到的晶体衍射分辨率为1.1 Å,属于原始正交空间群;而第二种条件下得到的晶体(结晶溶液中含有钙)衍射分辨率为2.93 Å,属于原始单斜空间群。确定α-11贾第素的详细原子结构将有助于更好地了解其生物学功能,并可能确定这类蛋白质是否是抗贾第虫病的潜在药物靶点。