摘要
In this paper the solution conformation of the response regulator proteins from Deinococcus radiodurans was studied by small-angle X-ray scattering （SAXS）. The SAXS curves of Dr-rrA in solutions were obtained at Beamline 1W2A of Beijing Synchrotron Radiation Facility （BSRF）. Two possible conformations of the response regulator proteins, compact and incompact conformations, have been represented by the known crystallographic structures. And theoretical solution scattering curves of the two possible conformations were calculated and fitted to the experimental scattering curve of Dr-rrA, respectively. The result indicates that the solution conformation of the response regulator proteins is inclined to the compact one, which is in agreement with the result of biochemical experiments.
In this paper the solution conformation of the response regulator proteins from Deinococcus radiodurans was studied by small-angle X-ray scattering （SAXS）. The SAXS curves of Dr-rrA in solutions were obtained at Beamline 1W2A of Beijing Synchrotron Radiation Facility （BSRF）. Two possible conformations of the response regulator proteins, compact and incompact conformations, have been represented by the known crystallographic structures. And theoretical solution scattering curves of the two possible conformations were calculated and fitted to the experimental scattering curve of Dr-rrA, respectively. The result indicates that the solution conformation of the response regulator proteins is inclined to the compact one, which is in agreement with the result of biochemical experiments.
基金
Supported by National Natural Science Foundation of China(10979005)
National Basic Research Program of China(2009CB918600)
