Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+ -transporting ATP synthase from Pyrococcus horikoshii OT3.
H+ -transporting ATP synthase (H+ -ATPase) is a multi-subunit complex which acts to produce ATP molecules. The catalytic subunit A of the archaeal-type H+ -ATPase from Pyrococcus horikoshii OT3 was cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method with MPD as a precipitant. X-ray intensity data were collected to 2.55 A resolution at beamline BL41XU of SPring-8. The crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 128.0, c = 104.7 A, and contain one molecule per asymmetric unit.
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Yuki
Y
Maegawa
Haduki
H
Morita
Min
M
Yao
Nobuhisa
N
Watanabe
Isao
I
Tanaka
D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D043902:Pyrococcus horikoshii / Q000201:enzymology*
D006180:Proton-Translocating ATPases