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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fu, Tian-Min Li, Dan Nan, Jie Li, Lanfen Xue, Yafeng Su, Xiao-Dong
Description	Author Affiliation: Fu TM ( College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.)
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.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 12
Volume Number	63
Language	English
Publisher	Wiley
Publisher Date	2007-12-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Protein-serine-threonine Kinases Chemistry Metabolism Ribosomal Protein S6 Kinases, 90-kda Crystallization Crystallography, X-ray Genetics Isolation & Purification Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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