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Updated: 09-12-10

Crystallization of Fructose 1,6-bisphosphatase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis

Naeem Rashid^1*, Masood Ahmed Siddiqui², Muhammad Saleem Haider¹ and Muhammad Arshad Javed¹

Abstract: The enzyme Fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.11) is one of the key enzymes of the gluconeogenic pathway. It hydrolyses fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate (Pilkis & Claus, 1991). Here we report the crystallization of FBPase from Thermococcus kodakaraensis. This FBPase consists of 375 amino acids, with a molecular weight of 42kDa, and was prepared using an Escherichia coli expression system. The purified recombinant FBPase was crystallised using the sitting drop vapour-diffusion method at 17°C. Crystals grew tetragonally and measured approximately 0.4 mm in the longest dimension.

¹School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore 54590, Pakistan

²Department of Chemistry, Balochistan University, Quetta, Pakistan. 

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