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

Barford, D., Keller, J. C. (1994) Co-crystallization of the catalytic subunit of the serine/threonine specific protein phosphatase 1 from human in complex with microcystin LR. J Mol Biol, 235 (2). pp. 763-6. ISSN 0022-2836 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8289294
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.

Item Type: Paper
Uncontrolled Keywords: Crystallization Crystallography, X-Ray Humans Peptides, Cyclic/ chemistry Phosphoprotein Phosphatase/ chemistry Research Support, Non-U.S. Gov't Serine Threonine
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein phosphatase
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Hengartner lab
CSHL labs > Stillman lab
Depositing User: Matt Covey
Date Deposited: 04 May 2015 14:50
Last Modified: 04 May 2015 14:50
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31477

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