Purification and crystallization of the CDK‐associated protein phosphatase KAP expressed in escherichia coli | Zendy

Hanlon Neil | Zendy; Barford David | Zendy

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Purification and crystallization of the CDK‐associated protein phosphatase KAP expressed in escherichia coli

Author(s) -

Hanlon Neil,

Barford David

Publication year - 1998

Publication title -

protein science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.353

H-Index - 175

eISSN - 1469-896X

pISSN - 0961-8368

DOI - 10.1002/pro.5560070233

Subject(s) - cyclin dependent kinase , escherichia coli , phosphatase , recombinant dna , microbiology and biotechnology , cyclin , biology , kinase , chemistry , biochemistry , enzyme , cell cycle , cell , gene

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 P6 1 22, or its enantiomorph P6 5 22, with unit cell dimensions a = b 74.5 Ǎ, c = 139.5 Ǎ.

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