Crystallization and crystallographic analysis of human NUDT16.
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.
Zhang
Jie
J
Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Gao
Feng
F
Zhang
Qianmin
Q
Chen
Qianying
Q
Qi
Jianxun
J
Yan
Jinghua
J
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D011755:Pyrophosphatases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D012315:RNA Caps / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D012342:RNA, Small Nuclear / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
D012315:RNA Caps; D012342:RNA, Small Nuclear; D011994:Recombinant Proteins; C523314:Nudt16 protein, human; D011755:Pyrophosphatases