Adenovirus structure by X-ray crystallography and electron microscopy.
Adenovirus structure by X-ray crystallography and electron microscopy.
复制标题
通过 X 射线晶体学和电子显微镜观察腺病毒结构。
DOI：
10.1007/978-3-642-79496-4_2
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发表时间：
1995
影响因子：
--
通讯作者：
Burnett,RM
中科院分区：
文献类型：
--
作者：
Stewart,PL;Burnett,RM
In the 40 years since the discovery of adenovirus, a wide range of biophysical and biochemical techniques have been applied to understanding the structure of the virion (Ginsberg1979; Philipson1983). Its size and complexity have presented a particular challenge, and this chapter describes a novel combination of two imaging techniques. Interpretation of the resultant images has relied on the wealth of earlier data. The aim has been to use X-ray crystallography to determine atomic structures of individual protein components and electron microscopy (EM) to determine the low-resolution structure of the intact complex. By accurately positioning the atomic structures within the reconstructed EM density and performing difference imaging, high-resolution structural information on the 150 x 106-Da complex has been obtained. In comparison with other mammalian viruses for which structures have been determined by X-ray crystallography alone, the adenovirus particle is much larger, roughly 18 times the mass of the picornaviruses (Rossmannet al. 1985; Hogleet al. 1985) and six times the mass of the polyoma virus SV40 (Liddingtonet al. 1991). Thus far, the atomic structure of only one complete adenovirus capsid component, hexon, has been determined (Robertset al. 1986; Athappillyet al. 1994). An early low-resolution structure of hexon (Burnettet al. 1985) was used to develop a model for hexon packing in the adenovirus capsid (Burnett1985).
