Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize.

Tsugumi Nakanishi; Yasushi Ohki; Jun'ichi Oda; Makoto Matsuoka; Kanzo Sakata; Hiroaki Kato

doi:10.1107/s0907444903026179

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Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize.

Tsugumi Nakanishi·Yasushi Ohki·Jun'ichi Oda·Makoto Matsuoka·Kanzo Sakata·Hiroaki Kato

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Abstract

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.

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Chromatography, Agarose Chromatography, Gel Cloning, Molecular Crystallization Crystallography, X-Ray DNA, Plant Escherichia coli Pyruvate, Orthophosphate Dikinase Recombinant Proteins Zea mays Journal Article Research Support, Non-U.S. Gov't

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Tsugumi Nakanishi, Yasushi Ohki, Jun'ichi Oda, Makoto Matsuoka, Kanzo Sakata, Hiroaki Kato. 2003-12-18. Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize.. https://doi.org/10.1107/s0907444903026179

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