The Scripps Research Institute, La Jolla, CA 92037, United States.
Curr Opin Virol. 2012 Apr;2(2):115-21. doi: 10.1016/j.coviro.2011.12.008. Epub 2012 Jan 18.
A detailed structural analysis of the entire human adenovirus capsid has been stymied by the complexity and size of this 150 MDa macromolecular complex. Over the past 10 years, the steady improvements in viral genome manipulation concomitant with advances in crystallographic techniques and data processing software has allowed structure determination of this virus by X-ray diffraction at 3.5 Å resolution. The virus structure revealed the location, folds, and interactions of major and minor (cement proteins) on the inner and outer capsid surface. This new structural information sheds further light on the process of adenovirus capsid assembly and virus-host cell interactions.
整个人类腺病毒衣壳的详细结构分析受到该 150MDa 大分子复合物的复杂性和大小的阻碍。在过去的 10 年中，病毒基因组操作的稳步改进伴随着晶体学技术和数据处理软件的进步，使得通过 X 射线衍射以 3.5Å 分辨率对该病毒的结构进行了确定。病毒结构揭示了主要和次要（胶凝蛋白）在衣壳内外表面的位置、折叠和相互作用。这些新的结构信息进一步阐明了腺病毒衣壳组装和病毒-宿主细胞相互作用的过程。
