title: Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase.
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.
authors: College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
authors: Tian-Min
authors: TM
authors: Fu
authors: Dan
authors: D
authors: Li
authors: Jie
authors: J
authors: Nan
authors: Lanfen
authors: L
authors: Li
authors: Yafeng
authors: Y
authors: Xue
authors: Xiao-Dong
authors: XD
authors: Su
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D038744:Ribosomal Protein S6 Kinases, 90-kDa / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D017346:Protein Serine-Threonine Kinases; C069329:RPS6KA1 protein, human; D038744:Ribosomal Protein S6 Kinases, 90-kDa