对锥虫次黄嘌呤磷酸核糖转移酶进行有限的蛋白酶解可产生能将X射线衍射至近原子分辨率的晶体。
Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution.
作者信息
Nieves-Alicea R, Focia P J, Craig S P, Eakin A E
机构信息
Department of Biochemistry, University of Puerto Rico, Medical Sciences Campus, San Juan, PR 00936-5067, USA.
出版信息
Biochim Biophys Acta. 1998 Nov 10;1388(2):500-5. doi: 10.1016/s0167-4838(98)00210-6.
Two crystal forms of the hypoxanthine phosphoribosyltransferase from Trypanosoma cruzi were grown and characterized. Proteolytic modification at the C-terminus of the recombinant enzyme yielded monoclinic crystals that diffract X-rays to higher resolution than the original, trigonal crystal form. Data from the monoclinic crystal form enabled determination of the crystal structure for the trypanosomal HPRT to 1.4 A resolution.
培养并表征了来自克氏锥虫的次黄嘌呤磷酸核糖基转移酶的两种晶体形式。对重组酶C端进行蛋白水解修饰后得到单斜晶体，其X射线衍射分辨率高于原始的三角晶体形式。单斜晶体形式的数据使得克氏锥虫HPRT的晶体结构得以确定，分辨率达到1.4埃。
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