Investigation of the topological shape of bovine serum albumin in solution by small-angle x-ray scattering at Beijing synchrotron radiation facility ⁄
Investigation of the topological shape of bovine serum albumin in solution by small-angle x-ray scattering at Beijing synchrotron radiation facility ⁄
复制标题
DOI：
10.1088/1674-1056/17/12/040
复制
发表时间：
2008-12
影响因子：
1.7
通讯作者：
Shu-Qiang Dong;Li-Qin Li-Li-Qin-Li-2236528518;Liu Peng;Yu-Hui Dong;Xi-Meng Chen
中科院分区：
文献类型：
--
作者：
Shu-Qiang Dong;Li-Qin Li-Li-Qin-Li-2236528518;Liu Peng;Yu-Hui Dong;Xi-Meng Chen
本文报道了在北京同步辐射装置新建的小角X射线散射实验站上，对无配体牛血清白蛋白溶液的拓扑形状进行了研究。得到了一条合适的散射曲线，其回旋半径的计算值为31.2A±0.25A（1A= 0.1nm），与其他人的结果一致。结果表明，用从头算方法得到的低分辨结构模型与人血清白蛋白的晶体结构拟合得很好。所有这些结果都显示了光束线应用于结构生物学研究的潜力。并对该电站的特点、存在的问题及今后的改进措施进行了探讨。
This paper reports that at a newly constructed small-angle x-ray scattering station of Beijing Synchrotron Radiation Facility, the topological shape of ligand-free bovine serum albumin in solution has been investigated. An appropriate scattering curve is obtained and the calculated value of the gyration radius is 31.2A±0.25A (1A=0.1 nm) which is coincident with other ones' results. It finds that the low-resolution structure models obtained by making use of ab initio reconstruction methods are fitting the crystal structure of human serum albumin very well. All of these results perform the potential of the beamline to apply to structural biology studies. The characteristics, the defects, and the improving measures of the station in future are also discussed.