Crystallization and preliminary x-ray diffraction studies of C4-form phosphoenolpyruvate carboxylase from maize.
Phosphoenolpyruvate carboxylase is a key enzyme in the fixation of atmospheric CO(2) in C(4) and crassulacean acid metabolism (CAM) plants. The enzyme catalyzes the irreversible carboxylation of phosphoenolpyruvate to form oxaloacetate and inorganic phosphate, the first committed step in the fixation of external CO(2) in these plants. The enzyme has been isolated from maize leaves and crystallized using the hanging-drop vapour-diffusion method with PEG 8000 as a precipitant at pH 7.5. The crystals belong to space group C222(1), with unit-cell dimensions a = 160.2, b = 175.6, c = 255.5 A, and diffract to 3.2 A resolution.
Matsumura
H
H
Department of Materials Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka, 565-0871, Japan.
Nagata
T
T
Terada
M
M
Shirakata
S
S
Inoue
T
T
Yoshinaga
T
T
Ueno
Y
Y
Saze
H
H
Izui
K
K
Kai
Y
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D010730:Phosphoenolpyruvate Carboxylase / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry; D011092:Polyethylene Glycols; D003313:Zea mays
D010940:Plant Proteins; D011092:Polyethylene Glycols; D010730:Phosphoenolpyruvate Carboxylase