Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography.
Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography.
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DOI：
10.1002/j.1460-2075.1989.tb08528.x
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发表时间：
1989-12
期刊：
影响因子：
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通讯作者：
Paul;S. Furcinittil;J. Oostrum;R. M. Burnett
中科院分区：
文献类型：
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作者：
Paul;S. Furcinittil;J. Oostrum;R. M. Burnett
腺病毒2型(AD2)的颗粒在分解时会持续产生九组(Gon)六角体，这是病毒粒子的主要外壳成分。用一种新的电子显微镜和X射线结晶学相结合的方法确定了Gon的一个次要成分(6%)的位置。布鲁克海文扫描电子显微镜(STEM)被用来估计蛋白质在GON中的分布，分辨率为15-18A。然后使用从X射线晶体结构得到的六邻子模型来搜索STEM图像，确定相对六邻子位置到1A以内。STEM图像和模型六角基团之间的差异图像显示了沿着六角-六角界面延伸的多肽IX的单个单体。这一分布证实了我们早先的建议，即四个三聚体多肽IX嵌入到Gon上表面的大空腔中，以粘合六角形形成高度稳定的组装。
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.