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

作者信息

Zhang F, Robbins D J, Cobb M H, Goldsmith E J

机构信息

Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas 75235-9038.

出版信息

J Mol Biol. 1993 Oct 5;233(3):550-2. doi: 10.1006/jmbi.1993.1532.

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 P2(1). The cell constants are a = 49.32 A, b = 71.42 A, c = 61.25 A, and beta = 109.75 degrees, and the crystals diffract to better than 1.8 A resolution.

摘要

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