Abstract
The extracellular signal-regulated kinase ERK2, a member of the protein kinase superfamily, phosphorylates a variety of cellular proteins in response to extracellular signals. ERK2 expressed in Escherichia coli as a fusion protein with the sequence Ala-His6 at the N terminus has low basal activity and very low levels of phosphate incorporation, but can be fully activated. The Ala-His6 ERK2 as expressed in the unphosphorylated form has been crystallized in space group P21. The cell constants are a=49.32 Å, b=71.42 Å, c=61.25 Å, and β=109.75°, and the crystals diffract to better than 1.8 Å resolution.
Original language | English (US) |
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Pages (from-to) | 550-552 |
Number of pages | 3 |
Journal | Journal of Molecular Biology |
Volume | 233 |
Issue number | 3 |
DOIs | |
State | Published - Jan 1 1993 |
Keywords
- Crystallization
- Extracellular signal-regulated kinases
- MAP kinases
- Phosphorylation
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology