Co-crystallization of the catalytic subunit of the serine/threonine specific protein phosphatase 1 from human in complex with microcystin LR

J Mol Biol. 1994 Jan 14;235(2):763-6. doi: 10.1006/jmbi.1994.1027.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Marine Toxins
  • Microcystins
  • Peptides, Cyclic / chemistry*
  • Phosphoprotein Phosphatases / chemistry*
  • Protein Phosphatase 1
  • Serine
  • Threonine

Substances

  • Marine Toxins
  • Microcystins
  • Peptides, Cyclic
  • Threonine
  • Serine
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1
  • cyanoginosin LR