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 (US)
Pages (from-to)550-552
Number of pages3
JournalJournal of Molecular Biology
Volume233
Issue number3
StatePublished - 1993

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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

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title = "Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag",
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 {\AA}, b=71.42 {\AA}, c=61.25 {\AA}, and β=109.75°, and the crystals diffract to better than 1.8 {\AA} resolution.",
keywords = "Crystallization, Extracellular signal-regulated kinases, MAP kinases, Phosphorylation",
author = "Faming Zhang and Robbins, {David J.} and Cobb, {Melanie H.} and Goldsmith, {Elizabeth J.}",
year = "1993",
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journal = "Journal of Molecular Biology",
issn = "0022-2836",
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T1 - Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag

AU - Zhang, Faming

AU - Robbins, David J.

AU - Cobb, Melanie H.

AU - Goldsmith, Elizabeth J.

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

KW - Crystallization

KW - Extracellular signal-regulated kinases

KW - MAP kinases

KW - Phosphorylation

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