Crystallization and preliminary X-ray analysis of inorganic pyrophosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
Inorganic pyrophosphatase (PPase; EC 3.6.1.1) from the hyperthermophile Pyrococcus horikoshii was crystallized by the hanging-drop vapour-diffusion method at pH 5.0 using polyethyleneglycol 4000 as the precipitant. The crystal belongs to space group P2(1)2(1)2, with unit-cell parameters a = 71.7, b = 86.5, c = 92.5 A, alpha = beta = gamma = 90 degrees. There are two molecules in the asymmetric unit. The crystals were stable during exposure to X-rays and a full set of X-ray diffraction data was collected to 2.7 A resolution in-house.
Liu
Binbin
B
Laboratory of Structural Biology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
Li
Xuemei
X
Gao
Renjun
R
Zhou
Weihong
W
Xie
Guiqiu
G
Bartlam
Mark
M
Pang
Hai
H
Feng
Yan
Y
Rao
Zihe
Z
D003460:Crystallization; D018360:Crystallography, X-Ray; D006863:Hydrogen-Ion Concentration; D043564:Inorganic Pyrophosphatase / Q000737:chemistry*; D011092:Polyethylene Glycols; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D043564:Inorganic Pyrophosphatase