Open AccessCrystallization and crystallographic analysis of human NUDT16
Author(s) -
Zhang Jie,
Gao Feng,
Zhang Qianmin,
Chen Qianying,
Qi Jianxun,
Yan Jinghua
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108016928
Subject(s) - crystallization , crystallography , recombinant dna , escherichia coli , resolution (logic) , molecule , diffusion , solvent , chemistry , materials science , biochemistry , thermodynamics , physics , gene , organic chemistry , artificial intelligence , computer science
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 P 2 1 2 1 2 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 3 Da −1 and 35.84%, respectively, for two molecules per asymmetric unit.