摘要
The bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphos-phosphatase was expressed in high yield Escherichia coli and purified to homogeneity. Single crystals of chicken liver bisphophatase domain suitable for X-ray diffraction were obtained by the hanging drop vapor diffusion method. The crystals belong to tetragonal space group P41212 or P43213 with two molecules per asymmetric unit. The determined cell dimensions are: a=b= 10.02 nm, c= 13.98 nm, α=β=г=90°. EHffraction data were collected on Weissenberg camera with synchrotron radiation at 0.32nm resolution.
The bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphos-phosphatase was expressed in high yield Escherichia coli and purified to homogeneity. Single crystals of chicken liver bisphophatase domain suitable for X-ray diffraction were obtained by the hanging drop vapor diffusion method. The crystals belong to tetragonal space group P41212 or P43213 with two molecules per asymmetric unit. The determined cell dimensions are: a=b= 10.02 nm, c= 13.98 nm, α=β=г=90°. EHffraction data were collected on Weissenberg camera with synchrotron radiation at 0.32nm resolution.
基金
Project supported by the Science Foundation of Chinese Academy of Sciences (KZ85-04), the Climbing Project of the State Commission of Science and Technology
the National Natural Science Foundation of China.
