Purification, crystallization and preliminary X-ray diffraction analysis of the fructose-1,6-/sedoheptulose-1,7-bisphosphatase of Synechococcus PCC 7942.
Fructose-1,6-/sedoheptulose-1,7-bisphosphatase of Synechococcus PCC 7942, overexpressed from Escherichia coli, has been purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals were monoclinic, with unit-cell parameters a = 80.1, b = 84.2, c = 104.3 A, beta = 101.7 degrees. They belonged to space group P2(1) and diffracted to at least 2.2 A resolution. The calculated V(M) value, based on a tetramer in the asymmetric unit, was 2.2 A(3) Da(-1).
Nakamura
Y
Y
Research Institute for Advanced Science and Technology, Osaka Prefecture University, Sakai, Osaka 599-8570, Japan. ynakam@biochem.osakafu-u.ac.jp
Tada
T
T
Wada
K
K
Kinoshita
T
T
Tamoi
M
M
Shigeoka
S
S
Nishimura
K
K
D003460:Crystallization; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation
D010744:Phosphoric Monoester Hydrolases; C022627:sedoheptulose-bisphosphatase