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The nitrilase-like (NIT) protein subfamily is a member of the nitrilase superfamily, which exhibits CN hydrolase activity. NIT proteins are highly conserved, and mammals have Nit1 and Nit2. Nit proteins are putative tumor suppressors; however, the enzymatic activities of Nit1 and Nit2 are different. Nit1 is a metabolite repair enzyme, whereas Nit2 is an ω-amidase. In this study, in order to understand the structural features and functional diversity of Nit proteins, Nit2 from Kluyveromyces lactis was crystallized, and X-ray diffraction data were obtained at a resolution of 2.2 Å. The crystal of K. lactis Nit2 (KlNit2) belonged to the space group C2, with the unit cell parameters a = 79.0 Å, b = 211.1 Å, c = 89.4 Å, α = γ = 90°, β = 112.1°. The crystal contained four macromolecules in the asymmetric unit.

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