Purification and crystallization of the CDK‐associated protein phosphatase KAP expressed in escherichia coli
Open Access
- 1 February 1998
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 7 (2) , 508-511
- https://doi.org/10.1002/pro.5560070233
Abstract
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 Ǎ resolution when exposed to synchrotron radiation and belong to space group P6122, or its enantiomorph P6522, with unit cell dimensions a= b 74.5 Ǎ, c = 139.5 Ǎ.Keywords
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