COCRYSTALLIZATION OF THE CATALYTIC SUBUNIT OF THE SERINE THREONINE SPECIFIC PROTEIN PHOSPHATASE-1 FROM HUMAN IN COMPLEX WITH MICROCYSTIN LR

被引:29
作者
BARFORD, D
KELLER, JC
机构
[1] W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724
关键词
PROTEIN PHOSPHATASE-1; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; PROTEIN PURIFICATION; PROTEIN CRYSTALLOGRAPHY;
D O I
10.1006/jmbi.1994.1027
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 å when exposed to synchrotron radiation and belong to space group P21212 with a = 109.5 å, b = 90.6 å, c = 38.7 å. 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. © 1994 Academic Press Limited.
引用
收藏
页码:763 / 766
页数:4
相关论文
共 32 条