Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize.
Pyruvate phosphate dikinase (PPDK) from maize catalyzes the reversible conversion of ATP, orthophosphate and pyruvate to AMP, pyrophosphate and PEP. In higher plants, this enzyme is believed to be involved in the C(4) dicarboxylic acid pathway. PPDK was crystallized by the vapour-diffusion method using polyethylene glycol as a precipitant. The crystals belong to the orthorhombic space group C2, with unit-cell parameters a = 108.2, b = 100.2, c = 108.4 A, beta = 96.5 degrees, and diffract to 2.3 A using SPring-8 synchrotron radiation.
Nakanishi
Tsugumi
T
Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
Ohki
Yasushi
Y
Oda
Jun'ichi
J
Matsuoka
Makoto
M
Sakata
Kanzo
K
Kato
Hiroaki
H
D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D018744:DNA, Plant / Q000737:chemistry / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D011772:Pyruvate, Orthophosphate Dikinase / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D003313:Zea mays / Q000201:enzymology* / Q000235:genetics
D018744:DNA, Plant; D011994:Recombinant Proteins; D011772:Pyruvate, Orthophosphate Dikinase