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

Tian-Min Fu; Dan Li; Jie Nan; Lanfen Li; Yafeng Xue; Xiao-Dong Su

doi:10.1107/S1744309107051329

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

Tian-Min Fu, Dan Li, Jie Nan, Lanfen Li, Yafeng Xue, Xiao-Dong Su

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	1026-8
Number of pages	3
Journal	Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	Pt 12
DOIs	https://doi.org/10.1107/S1744309107051329
Publication status	Published - 2007 Dec 1

Free keywords

Crystallization
Crystallography, X-Ray
Humans
Protein-Serine-Threonine Kinases
Ribosomal Protein S6 Kinases, 90-kDa

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10.1107/S1744309107051329

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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.",

keywords = "Crystallization, Crystallography, X-Ray, Humans, Protein-Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, 90-kDa",

author = "Tian-Min Fu and Dan Li and Jie Nan and Lanfen Li and Yafeng Xue and Xiao-Dong Su",

year = "2007",

month = dec,

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doi = "10.1107/S1744309107051329",

language = "English",

volume = "63",

pages = "1026--8",

journal = "Acta Crystallographica. Section F: Structural Biology and Crystallization Communications",

issn = "2053-230X",

publisher = "Wiley-Blackwell",

number = "Pt 12",

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Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase. / Fu, Tian-Min; Li, Dan; Nan, Jie et al.
In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, Vol. 63, No. Pt 12, 01.12.2007, p. 1026-8.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase

AU - Fu, Tian-Min

AU - Li, Dan

AU - Nan, Jie

AU - Li, Lanfen

AU - Xue, Yafeng

AU - Su, Xiao-Dong

PY - 2007/12/1

Y1 - 2007/12/1

N2 - 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.

AB - 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.

KW - Crystallization

KW - Crystallography, X-Ray

KW - Humans

KW - Protein-Serine-Threonine Kinases

KW - Ribosomal Protein S6 Kinases, 90-kDa

U2 - 10.1107/S1744309107051329

DO - 10.1107/S1744309107051329

M3 - Article

C2 - 18084084

SN - 2053-230X

VL - 63

SP - 1026

EP - 1028

JO - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

IS - Pt 12

ER -

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

Abstract

Free keywords

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