Investigation of the topological shape of bovine serum albumin in solution by small-angle x-ray scattering at Beijing synchrotron radiation facility
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
aNuclear Science and Technology Department of Lanzhou University, Lanzhou 730000, China; bInstitute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China
Abstract 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 31.2ű0.25Å (1 Å=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.
Received: 03 February 2008
Revised: 08 September 2008
Accepted manuscript online:
PACS:
87.64.Bx
(Electron, neutron and x-ray diffraction and scattering)
Fund: Project supported by the Chinese
Academy of Science Innovation Key Project (Grant No KJCX2-SW-N06).
Cite this article:
Dong Shu-Qiang (董淑强), Li Li-Qin (李丽琴), Liu Peng (刘鹏), Dong Yu-Hui (董宇辉), Chen Xi-Meng(陈熙萌) Investigation of the topological shape of bovine serum albumin in solution by small-angle x-ray scattering at Beijing synchrotron radiation facility 2008 Chin. Phys. B 17 4574
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