中国物理B ›› 2008, Vol. 17 ›› Issue (12): 4574-4579.doi: 10.1088/1674-1056/17/12/040

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Investigation of the topological shape of bovine serum albumin in solution by small-angle x-ray scattering at Beijing synchrotron radiation facility

李丽琴1, 刘鹏1, 董宇辉1, 陈熙萌2, 董淑强3   

  1. (1)Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China; (2)Nuclear Science and Technology Department of Lanzhou University, Lanzhou 730000, China; (3)Nuclear Science and Technology Department of Lanzhou University, Lanzhou 730000, China;Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China
  • 收稿日期:2008-02-03 修回日期:2008-09-08 出版日期:2008-12-20 发布日期:2008-12-20
  • 基金资助:
    Project supported by the Chinese Academy of Science Innovation Key Project (Grant No KJCX2-SW-N06).

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)bChen Xi-Meng(陈熙萌)a   

  1. a Nuclear Science and Technology Department of Lanzhou University, Lanzhou 730000, China; b Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China
  • Received:2008-02-03 Revised:2008-09-08 Online:2008-12-20 Published:2008-12-20
  • Supported by:
    Project supported by the Chinese Academy of Science Innovation Key Project (Grant No KJCX2-SW-N06).

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.

关键词: small-angle x-ray scattering, ab initio methods, bovine serum albumin, Beijing synchrotron radiation facility

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.

Key words: small-angle x-ray scattering, ab initio methods, bovine serum albumin, Beijing synchrotron radiation facility

中图分类号:  (Electron, neutron and x-ray diffraction and scattering)

  • 87.64.Bx
87.14.E- (Proteins) 87.15.B- (Structure of biomolecules) 87.15.N- (Properties of solutions of macromolecules)