Amzel L M, Pedersen P L
J Biol Chem. 1978 Apr 10;253(7):2067-9.
The homogeneous rat liver F1-ATPase preparation of Catterall and Pedersen (Catterall, W.A., and Pedersen, P.L. (1971) J. Biol. Chem. 246, 4987-4994) has been crystallized from a solution containing phosphate and ATP by precipitation with ammonium sulfate. Most of the resultant crystals are cubes of approximately 0.3 to 0.6 mm per side. X-ray precession photographs show that the crystals are rhombohedral, space group R32 (D37 NO155) with hexagonal cell dimensions a = 148 A, c = 368 A. The molecular weight of the asymmetric unit of the crystals is 190,000 or about half the molecular weight (384,000) of the rat liver enzyme indicating that the crystallographic 2-fold axes of symmetry coincide with a molecular symmetry axis. The crystals diffract to at least 3.5 A and therefore this is the first report of an ATPase preparation in which crystals suitable for x-ray analysis have been obtained.
卡特拉尔（Catterall）和佩德森（Pedersen）制备的大鼠肝脏F1 - ATP酶均一制剂（卡特拉尔，W.A.，和佩德森，P.L.（1971年）《生物化学杂志》246，4987 - 4994），已通过用硫酸铵沉淀，从含有磷酸盐和ATP的溶液中结晶出来。所得晶体大多为边长约0.3至0.6毫米的立方体。X射线进动照片显示，这些晶体为菱面体，空间群为R32（D37 NO155），六方晶胞尺寸a = 148 Å，c = 368 Å。晶体不对称单元的分子量为190,000，约为大鼠肝脏酶分子量（384,000）的一半，这表明晶体学的二重对称轴与分子对称轴重合。这些晶体的衍射能力至少达到3.5 Å，因此这是关于一种ATP酶制剂的首次报道，其中已获得适合X射线分析的晶体。
