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Crystallization and crystallographic analysis of human NUDT16.

ABSTRACT: 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 A resolution, belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.47, b = 79.32, c = 97.20 A. The Matthews coefficient and the solvent content were calculated to be 1.92 A(3) Da(-1) and 35.84%, respectively, for two molecules per asymmetric unit.

SUBMITTER: Zhang J

PROVIDER: S-EPMC2443980 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Crystallization and crystallographic analysis of human NUDT16.

Zhang Jie J Gao Feng F Zhang Qianmin Q Chen Qianying Q Qi Jianxun J Yan Jinghua J

Acta crystallographica. Section F, Structural biology and crystallization communications 20080611 Pt 7

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 A resolution, belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.47, b = 79.32, c = 97.20 A. The Matthews coefficient and the solvent content were calculated to be 1.92 A(3) Da(-1) and 35.84%, respectively, for t ...[more]

PMID: 18607096

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