Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis.
Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis.
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DOI：
10.1083/jcb.86.1.327
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发表时间：
1980-07
期刊：
影响因子：
--
通讯作者：
Rosenbusch JP
中科院分区：
文献类型：
--
作者：
Garavito RM;Rosenbusch JP
基质蛋白（Matrix protein）是一种跨大肠杆菌外膜的成孔跨膜蛋白，它具有多种三维晶体结构，可以用电子显微镜和X射线分析。成功地结合成大晶体取决于使用α-辛基葡糖苷，这是一种对蛋白质亲和力相对较低的去污剂。薄片晶体的电子显微照片显示出高度的有序性。初步的晶体学数据表明，显示衍射至3.8 A的晶体具有立方空间群。
Matrix protein, a pore-forming transmembrane protein spanning the outer membrane of Escherichia coli, has been obtained in a variety of three- dimensional crystal forms amenable to both electron microscope and x- ray analyses. Successful association into large crystals depended on the use of alpha-octyl glucoside, a detergent with relatively low affinity for the protein. Electron micrographs of thin-sectioned crystals show a high degree of order. Preliminary crystallographic data suggest that the crystals, which exhibit diffraction to 3.8 A, have a cubic space group.