Co-crystallization of the catalytic subunit of the serine/threonine specific protein phosphatase 1 from human in complex with microcystin LR.
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.
Barford
D
D
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, NY 11724.
Keller
J C
JC
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008387:Marine Toxins; D052998:Microcystins; D010456:Peptides, Cyclic / Q000737:chemistry*; D010749:Phosphoprotein Phosphatases / Q000737:chemistry*; D054645:Protein Phosphatase 1; D012694:Serine; D013912:Threonine
D008387:Marine Toxins; D052998:Microcystins; D010456:Peptides, Cyclic; D013912:Threonine; D012694:Serine; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; C057862:cyanoginosin LR