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 Scopus citations

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 (US)
Pages (from-to)550-552
Number of pages3
JournalJournal of molecular biology
Volume233
Issue number3
DOIs
StatePublished - Jan 1 1993

Keywords

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

ASJC Scopus subject areas

  • Virology

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