Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase
(2007) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 63(Pt 12). p.8-1026- 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.
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https://lup.lub.lu.se/record/ac1dbddd-5583-4042-a39e-8c9e1673f595
- author
- Fu, Tian-Min ; Li, Dan ; Nan, Jie LU ; Li, Lanfen ; Xue, Yafeng and Su, Xiao-Dong LU
- organization
- publishing date
- 2007-12-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Crystallization, Crystallography, X-Ray, Humans, Protein-Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, 90-kDa
- in
- Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
- volume
- 63
- issue
- Pt 12
- pages
- 3 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:36849085969
- pmid:18084084
- ISSN
- 2053-230X
- DOI
- 10.1107/S1744309107051329
- language
- English
- LU publication?
- yes
- id
- ac1dbddd-5583-4042-a39e-8c9e1673f595
- date added to LUP
- 2016-09-07 22:53:56
- date last changed
- 2025-01-12 11:01:41
@article{ac1dbddd-5583-4042-a39e-8c9e1673f595, abstract = {{<p>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.</p>}}, author = {{Fu, Tian-Min and Li, Dan and Nan, Jie and Li, Lanfen and Xue, Yafeng and Su, Xiao-Dong}}, issn = {{2053-230X}}, keywords = {{Crystallization; Crystallography, X-Ray; Humans; Protein-Serine-Threonine Kinases; Ribosomal Protein S6 Kinases, 90-kDa}}, language = {{eng}}, month = {{12}}, number = {{Pt 12}}, pages = {{8--1026}}, publisher = {{Wiley-Blackwell}}, series = {{Acta Crystallographica. Section F: Structural Biology and Crystallization Communications}}, title = {{Protein preparation, crystallization and preliminary X-ray analysis of the C-terminal domain of human RSK1 serine/threonine protein kinase}}, url = {{http://dx.doi.org/10.1107/S1744309107051329}}, doi = {{10.1107/S1744309107051329}}, volume = {{63}}, year = {{2007}}, }