Bentley G A, Lewit-Bentley A, Liljas L, Skoglund U, Roth M, Unge T
J Mol Biol. 1987 Mar 5;194(1):129-41. doi: 10.1016/0022-2836(87)90722-4.
The crystal structure of satellite tobacco necrosis virus has been studied by neutron diffraction at 16 A resolution using the technique of 1H2O/2H2O solvent contrast variation to distinguish between the regions of protein and nucleic acid. The RNA density is essentially localized in a region just inside the protein coat, leading to a significant interaction between the two components. From the appearance of the RNA density we conclude that the protein coat imposes partial icosahedral symmetry on a significant proportion of the nucleic acid. The shape and dimensions of the major part of this density suggests that about 72% of the total RNA could be double-helical in structure. The most important interaction between the two components of the virus occurs between the N-terminal triple-helical arms of the protein subunits and those regions of the RNA density that could have a double-helical secondary structure.
利用(^{1}H_{2}O/^{2}H_{2}O)溶剂对比度变化技术，通过16埃分辨率的中子衍射研究了卫星烟草坏死病毒的晶体结构，以区分蛋白质和核酸区域。RNA密度基本上定位在蛋白质外壳内部的一个区域，导致这两个组分之间发生显著相互作用。从RNA密度的外观来看，我们得出结论，蛋白质外壳对相当一部分核酸施加了部分二十面体对称性。该密度主要部分的形状和尺寸表明，总RNA中约72%的结构可能是双螺旋的。病毒两个组分之间最重要的相互作用发生在蛋白质亚基的N端三螺旋臂与RNA密度中可能具有双螺旋二级结构的区域之间。
