Furcinitti P S, van Oostrum J, Burnett R M
Biology Department, Brookhaven National Laboratory, Upton, NY 11973.
EMBO J. 1989 Dec 1;8(12):3563-70. doi: 10.1002/j.1460-2075.1989.tb08528.x.
Particles of adenovirus type 2 (ad2), when disassembled, consistently yield groups-of-nine (GON) hexons, which are the major virion shell component. The location of a minor component (6%) of the GON has been determined using a novel combination of electron microscopy and X-ray crystallography. The Brookhaven Scanning Transmission Electron Microscope (STEM) was used to estimate the distribution of protein in the GON to a resolution of 15-18 A. The relative hexon positions then were determined to within 1 A using a model of the hexon derived from the X-ray crystal structure to search the STEM image. The difference image between the STEM image and a model hexon group reveals individual monomers of polypeptide IX extending along the hexon--hexon interfaces. The distribution confirms our earlier proposal that four trimers of polypeptide IX are embedded in the large cavities in the upper surface of the GON to cement hexons into a highly-stable assembly.
2型腺病毒（Ad2）颗粒在拆解时，始终会产生九聚体（GON）六邻体，它们是病毒体外壳的主要成分。利用电子显微镜和X射线晶体学的新组合，已确定了GON中一种次要成分（6%）的位置。布鲁克海文扫描透射电子显微镜（STEM）用于估计GON中蛋白质的分布，分辨率为15 - 18埃。然后，使用从X射线晶体结构衍生的六邻体模型在STEM图像中搜索，将六邻体的相对位置确定在1埃以内。STEM图像与六邻体模型组之间的差异图像揭示了沿着六邻体 - 六邻体界面延伸的多肽IX的单个单体。这种分布证实了我们之前的提议，即四个多肽IX三聚体嵌入GON上表面的大腔中，将六邻体粘结成高度稳定的组装体。
