Barford D, Keller J C
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, NY 11724.
J Mol Biol. 1994 Jan 14;235(2):763-6. doi: 10.1006/jmbi.1994.1027.
The catalytic subunit of the serine/threonine specific protein phosphatase 1 from human (molecular mass 37 KDa) has been co-crystallized in complex with the cyanobacterial toxin microcystin LR (molecular mass 1 kDa). The crystals diffract to a resolution of 2.8 A when exposed to synchrotron radiation and belong to space group P2(1)2(1)2 with a = 109.5 A, b = 90.6 A, c = 38.7 A. There is one molecule of protein phosphatase 1 per asymmetric unit. The crystal form is suitable for the determination of the atomic structure of protein phosphatase 1.
人源丝氨酸/苏氨酸特异性蛋白磷酸酶1的催化亚基（分子量37千道尔顿）已与蓝藻毒素微囊藻毒素LR（分子量1千道尔顿）形成复合物并进行了共结晶。当暴露于同步辐射时，晶体的衍射分辨率达到2.8埃，属于空间群P2(1)2(1)2，a = 109.5埃，b = 90.6埃，c = 38.7埃。每个不对称单元中有一个蛋白磷酸酶1分子。这种晶体形式适合用于确定蛋白磷酸酶1的原子结构。
