Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase

Research output: Contribution to journalArticle

Abstract

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 A and belonged to space group P2(1), with unit-cell parameters a = 39.8, b = 143.8, c = 59.9 A, beta = 95.7 degrees.

Details

Authors
  • Tian-Min Fu
  • Dan Li
  • Jie Nan
  • Lanfen Li
  • Yafeng Xue
  • Xiao-Dong Su
Organisations
Research areas and keywords

Keywords

  • Crystallization, Crystallography, X-Ray, Humans, Protein-Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, 90-kDa
Original languageEnglish
Pages (from-to)1026-8
Number of pages3
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications
Volume63
Issue numberPt 12
Publication statusPublished - 2007 Dec 1
Publication categoryResearch
Peer-reviewedYes