Crystallization and crystallographic analysis of human NUDT16

摘要

Human NUDT16, a decapping enzyme belonging to the Nudix superfamily, plays a pivotal role in U8 snoRNA stability. Recombinant NUDT16 expressed in Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. The crystals, which diffracted to 2.10 Å resolution, belonged to space group P212121, with unit-cell parameters a = 44.47, b = 79.32, c = 97.20 Å. The Matthews coefficient and the solvent content were calculated to be 1.92 ų Da⁻¹ and 35.84%, respectively, for two molecules per asymmetric unit.