Crystallization and preliminary neutron diffraction studies of ADP-ribose pyrophosphatase-I from Thermus thermophilus HB8.
ADP-ribose pyrophosphatase-I from Thermus thermophilus HB8 (TtADPRase-I) prevents the intracellular accumulation of ADP-ribose by hydrolyzing it to AMP and ribose 5'-phosphate. To understand the catalytic mechanism of TtADPRase-I, it is necessary to investigate the role of glutamates and metal ions as well as the coordination of water molecules located at the active site. A macroseeding method was developed in order to obtain a large TtADPRase-I crystal which was suitable for a neutron diffraction study to provide structural information. Neutron and X-ray diffraction experiments were performed at room temperature using the same crystal. The crystal diffracted to 2.1 and 1.5 Å resolution in the neutron and X-ray diffraction experiments, respectively. The crystal belonged to the primitive space group P3(2)21, with unit-cell parameters a = b = 50.7, c = 119 Å.
Quantum Beam Science Directorate, Japan Atomic Energy Agency, 4 Shirakata-Shirane, Tokai, Ibaraki 319-1195, Japan.
Nobuo
N
Okazaki
Motoyasu
M
Adachi
Taro
T
Tamada
Kazuo
K
Kurihara
Takushi
T
Ooga
Nobuo
N
Kamiya
Seiki
S
Kuramitsu
Ryota
R
Kuroki
D003460:Crystallization; D033363:Neutron Diffraction; D011755:Pyrophosphatases / Q000737:chemistry*; D016963:Thermus thermophilus / Q000201:enzymology*
C058796:ADP-ribose pyrophosphatase I; D011755:Pyrophosphatases