Crystallization and Preliminary X-Ray Crystallographic Studies of Trypanosoma brucei Prostaglandin F2.ALPHA. Synthase.

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概要

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• Prostaglandin F2α is a potent mediator of various physiological and pathological processes. Trypanosoma brucei prostaglandin F2α synthase (TbPGFS) catalyzes the NADPH-dependent reduction of 9, 11-endoperoxide PGH2 to PGF2α, and could thus be involved in the elevation of the PGF2α concentration during African trypanosomasis. In the present report, the purification and crystallization of recombinant TbPGFS are described. The active recombinant enzyme was crystallized by the hanging-drop vapor-diffusion method using ammonium sulfate as a precipitant. The crystal belonged to a tetragonal space group, P41212 or P43212, with unit-cell parameters of a=b=112.3 Å, and c=140.0 Å. Native data up to 2.6 Å resolution were collected from the crystal using our home facility.

• 社団法人 日本生化学会の論文

著者

• Kai Yasushi

  Department Of Applied Chemistry Faculty Of Engineering Osaka University

• Kubata Bruno

  Department Of Molecular Behavioral Biology Japan Science And Technology Corporation Osaka Bioscience

• Kabututu Zakayi

  Department Of Molecular Behavioral Biology Osaka Bioscience Institute

• Matsumura Hiroyoshi

  Department Of Applied Chemistry Graduate School Of Engineering Osaka University

• Urade Yoshihiro

  Department Of Behavioral Biology Osaka Bioscience Institute

• Inoue Tsuyoshi

  Department Of Appied Chemistry Faculty Of Engineering Osaka University

• Kubata Bruno

  Department of Molecular Behavioral Biology Japan Science and Technology Corporation, Osaka Bioscience Institute

• Okano Yousuki

  Department of Materials Chemistry , Graduate School of Engineering, Osaka University Japan Science and Technology Corporation, Osaka Bioscience Institute

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