Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag

Faming Zhang, David J Robbins, Melanie H. Cobb, Elizabeth J. Goldsmith

Research output: Contribution to journalArticle

26 Citations (Scopus)

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 languageEnglish
Pages (from-to)550-552
Number of pages3
JournalJournal of Molecular Biology
Volume233
Issue number3
StatePublished - Dec 1 1993
Externally publishedYes

Fingerprint

Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase Kinases
Extracellular Signal-Regulated MAP Kinases
Crystallization
X-Rays
Protein Kinases
Proteins
Phosphates
Escherichia coli

Keywords

  • Crystallization
  • Extracellular signal-regulated kinases
  • MAP kinases
  • Phosphorylation

ASJC Scopus subject areas

  • Virology

Cite this

Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag. / Zhang, Faming; Robbins, David J; Cobb, Melanie H.; Goldsmith, Elizabeth J.

In: Journal of Molecular Biology, Vol. 233, No. 3, 01.12.1993, p. 550-552.

Research output: Contribution to journalArticle

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