Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase
Journal Article
·
· Acta Crystallographica. Section F
- College of Life Sciences, Peking University, Beijing 100871 (China)
- AstraZeneca Global Structural Chemistry, AstraZeneca R&D Molndal, SE-431 83, Molndal (Sweden)
The C-terminal catalytic domain of serine/threonine kinase RSK1 has been crystallized; the crystals diffracted to a resolution of 2.7 Å and belonged to space group P2{sub 1}. As a substrate of extracellular signal-related kinase (ERK), the p90 ribosome S6 kinase 1 (RSK1) is at the terminus of the Ras/ERK pathway. Residues 411–735 of human RSK1, covering the C-terminal serine/threonine kinase catalytic domain and the functionally important tail, were cloned into an Escherichia coli expression vector. The protein was expressed, purified and crystallized. The crystals diffracted to 2.7 Å and belonged to space group P2{sub 1}, with unit-cell parameters a = 39.8, b = 143.8, c = 59.9 Å, β = 95.7°.
- OSTI ID:
- 22360451
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 12 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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