チトクロム酸化酵素の結晶化
スポンサーリンク
概要
- 論文の詳細を見る
The three dimensional structure of cytochrome c oxidase, a integral mitochondrial membrane protein complex, is critical to elucidation of the mechanism of the enzyme reactions. The crystallization of the enzyme isolated from bovine hearts has been tried under various conditions (exp. ionic strength, detergents, precipitants) . At low inoic strength (1-3mM Na-Pi buffer, pH 7.4), increasing the detergent (Brij-35) concentration was successful in producing the hexagonal bipyramidal crystals with typical dimension of 0.5 mm which diffracted X-rays at a resolution of 7 Å. On the other hand, at high ionic strength (100mM Na-Pi buffer, pH 7.4, 33% sat. AmSO<SUB>4</SUB>) the tetragonal crystals were obtained, which contain BL8SY as the detergent. The tetragonal crystals diffracted X-rays at 5-6Å resolution under anaerobic conditions.
- 日本結晶学会の論文