Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2.

Academic Article

Abstract

  • Rng2 is a multidomain protein component of the actiomyosin ring and the spindle pole body necessary for cytokinesis in Schizosaccharomyces pombe. The calponin-homology domain of Rng2 from S. pombe has been overexpressed, purified and crystallized. The crystals belong to space group P2(1). Br- and Hg-derivative data sets were measured to 2.21 A using synchrotron radiation from crystals that were partially fixed with glutaraldehyde. Electron-density maps have been obtained from two-wavelength MAD on the Br derivative and SAD on the Hg derivative.

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    Published In

    Keywords

  • Calcium-Binding Proteins, Cell Cycle Proteins, Crystallization, Crystallography, X-Ray, GTPase-Activating Proteins, Microfilament Proteins, Protein Structure, Tertiary, Recombinant Fusion Proteins, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Static Electricity, Synchrotrons, Thrombin

    • Digital Object Identifier (doi)

    Author List

  • Wang C-H; Walsh M; Balasubramanian MK; Dokland T

    • Start Page

  • 1809

    • End Page

  • 1812

    • Volume

  • 59

    • Issue

  • Pt 10