Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase.
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.
Fu
Tian-Min
TM
College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Li
Dan
D
Nan
Jie
J
Li
Lanfen
L
Xue
Yafeng
Y
Su
Xiao-Dong
XD
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*
D017346:Protein Serine-Threonine Kinases; C069329:RPS6KA1 protein, human; D038744:Ribosomal Protein S6 Kinases, 90-kDa