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Protein Science, Vol 7, Issue 2 508-511, Copyright © 1998 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Purification and crystallization of the CDK-associated protein phosphatase KAP expressed in Escherichia coli

N. HANLON and D. BARFORD
Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, South Parks Road, Oxford, OX1 3QU, United Kingdom

The kinase associated phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates the cell cycle control protein, cyclin dependent kinase-2 on Thr 160 in a cyclin dependent manner (Poon & Hunter, 1995). We report here the over-expression of KAP in Escherichia coli as an N-terminal His-tagged protein using a modified pET-28a T7-expression vector. The recombinant protein was purified to homogeneity and crystallized. The crystals diffract to 2.3 A resolution when exposed to synchrotron radiation and belong to space group P6(1)22, or its enantiomorph P6(5)22, with unit cell dimensions a = b = 74.5 A, c = 139.5 A.
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