PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF RECOMBINANT CHICKEN LIVER FRUCTOSE-2,6-BISPHOSPHATASE

The bisphosphatase domain of chicken liver phofructo-2-kinase/fructose -2,6-bisphosphosphatase was expressed in high yield Escherichia coli a nd purified to homogeneity. Single crystals of chicken liver bisphopha tase domain suitable for X-ray diffraction were obtained by the hangin g drop The crystals belong to tetragonal space group P(4)2(1)2 or P4(3 )2(1)3 with two molecules per asymmetric unit. The determined cell dim ensions are: a=b=10.02 nm, c=13.98 nm, alpha=beta=Gamma=90 degrees Dif fraction data were collected on Weissenberg camera with synchrotron ra diation at 0.32 nm resolution.