Abstract
The apo form of the double mutant of Wolinella succinogenes L-asparaginase (WAS) with V23Q and K24T substitutions in the flexible N-terminal loop (WASm), which exhibits an order of magnitude lower glutaminase activity compared to the wild-type enzyme, was crystallized in two modifications (sp. grs. P22121 and P21). The three-dimensional structure in two modifications was determined at 1.5 and 1.7 A resolution, respectively. The three-dimensional structures and the molecular packing modes of the enzyme in two crystal modifications (monoclinic, sp. gr. P21, and orthorhombic, sp. gr. P22121) are compared. Intermolecular contacts and solvent channels in both crystal lattices are described. The orthorhombic crystals have a closer packing compared to the monoclinic crystals and lower water content (36.95 and 44.53%, respectively). However, the active sites in both structures are solvent accessible.
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