Crystallization and crystallographic analysis of human NUDT16

Journal Article · Tue Jul 01 00:00:00 EDT 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309108016928· OSTI ID:22360600

Zhang, Jie ^[1]; Gao, Feng ^[2]; Zhang, Qianmin ^[1]; Chen, Qianying ^[3]; Qi, Jianxun ^[4]; Yan, Jinghua ^[1]

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1. Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101 (China)
2. Institute of Biophysics, Chinese Academy of Sciences, Beijing 100080 (China)
3. Anhui Agricultural University, Anhui 230036 (China)
4. Institute of Physics, Chinese Academy of Sciences, Beijing 100080 (China)

Recombinant NUDT16 from human was expressed, purified and crystallized. The native crystals diffracted to 2.1 Å. 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 P2{sub 1}2{sub 1}2{sub 1}, 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 Å{sup 3} Da{sup −1} and 35.84%, respectively, for two molecules per asymmetric unit.

• OSTI ID: 22360600
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DIFFUSION
ESCHERICHIA COLI
MOLECULES
RESOLUTION
SOLVENTS
SPACE GROUPS
STABILITY