中国物理B ›› 2008, Vol. 17 ›› Issue (12): 4574-4579.doi: 10.1088/1674-1056/17/12/040
李丽琴1, 刘鹏1, 董宇辉1, 陈熙萌2, 董淑强3
Dong Shu-Qiang (董淑强)ab, Li Li-Qin (李丽琴)b, Liu Peng (刘鹏)b, Dong Yu-Hui (董宇辉)b, Chen Xi-Meng(陈熙萌)a
摘要: 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 31.2?±0.25? (1?=0.1nm) 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.
中图分类号: (Electron, neutron and x-ray diffraction and scattering)