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. 1998 Feb;7(2):508-11.
doi: 10.1002/pro.5560070233.

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

N Hanlon  1 , D Barford
Affiliations

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

N Hanlon et al. Protein Sci. 1998 Feb.

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 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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References

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