Crystallization and preliminary crystallographic analysis of the snake muscle fructose 1,6-bisphosphatase.
The snake muscle fructose 1,6-bisphosphatase, a typical allosteric enzyme which plays important roles in gluconeogenesis, was crystallized in the presence of polyethylene glycol 3350 and magnesium chloride at pH 8.5. The crystals diffract to 2.3 A on a rotating-anode X-ray source. The space group was determined to be either P3121 or its enantiomorph P3221, with unit-cell parameters a = b = 83.7, c = 202.41 A, alpha = beta = 90 and gamma = 120 degrees. There are two subunits in the asymmetric unit. Preliminary molecular-replacement studies indicate that the first enantiomorph is the correct one.
Zhu
D W
DW
The Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Quebec, G1V 4G2, Canada.
Xu
G J
GJ
Rehse
P H
PH
Azzi
A
A
Zhao
F K
FK
Lin
S X
SX
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D006597:Fructose-Bisphosphatase / Q000737:chemistry*; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D012911:Snakes
D006597:Fructose-Bisphosphatase