嗜热栖热放线菌甲硫氨酸氨基肽酶的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of methionine aminopeptidase from the hyperthermophilic bacterium Pyrococcus furiosus.
作者信息
Tahirov T H, Oki H, Tsukihara T, Ogasahara K, Izu Y, Tsunasawa S, Kato I, Yutani K
机构信息
Institute for Protein Research, Osaka University, Suita, Japan.
出版信息
Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):798-801. doi: 10.1107/S0907444997006793.
Methionine aminopeptidase (MAP) from Pyrococcus furiosus (Pfu) has been crystallized in four different forms (A, B, C and D). Form A crystals belong to space group P2(1) with unit-cell dimensions a = 54.18, b = 85.72, c = 72.84 A, beta = 108.34 degrees. Forms B, C and D belong to space group P6(2(4)) with unit-cell dimensions a = 139.1, c = 63.7 A for form B, a = 198.6, c = 243.8 A for form C, and a = 111.0, c = 125.0 A for form D. Forms A and D diffract to 2.9 A, form B diffracts to 3.5 A, and form C crystals diffract to 4.5 A. Form A contains two molecules of MAP-Pfu per asymmetric unit. The binuclear metal center positions and a non-crystallographic twofold symmetry matrix has been determined for the form A crystals.
来自嗜热栖热菌（Pfu）的甲硫氨酸氨肽酶（MAP）已以四种不同形式（A、B、C和D）结晶。A 型晶体属于空间群 P2(1)，晶胞参数为 a = 54.18、b = 85.72、c = 72.84 Å，β = 108.34°。B、C和D型属于空间群P6(2(4))，B型晶胞参数为a = 139.1、c = 63.7 Å，C型为a = 198.6、c = 243.8 Å，D型为a = 111.0、c = 125.0 Å。A型和D型晶体的衍射分辨率为2.9 Å，B型为3.5 Å，C型晶体为4.5 Å。每个不对称单元中，A型含有两个MAP-Pfu分子。已确定了A型晶体的双核金属中心位置和一个非晶体学二重对称矩阵。
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