Preliminary X-ray analysis of a truncated form of recombinant fructose-2,6-bisphosphatase
The bisphosphatase domain of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and a C-terminal 30 amino acid truncated form were expressed in high yield in Escherichia coli and purified to homogeneity. The separately expressed bisphosphatase domain and its C-terminal truncated form had kinetic properties similar to the bisphosphatase of the intact bifunctional enzyme, but their turnover numbers were fourfold higher. The truncated enzyme crystallized in space group P1 with two molecules per asymmetric unit. The determined cell dimensions are: a = 41.9 Å, b = 43.5 Å, c = 57.6 Å, α = 95.2°, β = 99.3°, and γ = 106.2°. These crystals diffract to 2.0 Å resolution when exposed to synchrotron radiation and are suitable for crystallographic structure analysis. © 1994 Academic Press Limited.
Publication Source (Journal or Book title)
Journal of Molecular Biology
Lee, Y., Lin, K., Okar, D., Alfano, N., Sarma, R., Pflugrath, J., & Pilkis, S. (1994). Preliminary X-ray analysis of a truncated form of recombinant fructose-2,6-bisphosphatase. Journal of Molecular Biology, 235 (3), 1147-1151. https://doi.org/10.1006/jmbi.1994.1065