Abstract
The Vitis vinifera dual-activity fucose and nucleotide-sugar metabolizing enzyme L-fucokinase:GDP-fucose pyrophosphorylase (FKP) has been purified to homogeneity and the 118.8 kDa monomeric protein has been crystallized by vapor diffusion in Zeppezauer tubes at 277 K. Crystals of the apoenzyme diffracted to 2.6 Å resolution and belonged to the tetragonal space group P4(1)2(1)2. There is a single FKP monomer in the asymmetric unit, giving a Matthews coefficient of 3.22 Å(3) Da(-1) and a solvent content of 61.8%. A complete native data set has been collected as a first step in determining the three-dimensional structure of this enzyme.
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Schedule a callMore From: Acta crystallographica. Section F, Structural biology and crystallization communications
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