Literature DB >> 14501122

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

Chern-Hoe Wang1, Martin Walsh, Mohan K Balasubramanian, Terje Dokland.   

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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Year:  2003        PMID: 14501122     DOI: 10.1107/s0907444903016123

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Stabilization of porcine pancreatic elastase crystals by glutaraldehyde cross-linking.

Authors:  Stefan Hofbauer; José A Brito; Jalmira Mulchande; Przemyslaw Nogly; Miguel Pessanha; Rui Moreira; Margarida Archer
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-09-23       Impact factor: 1.056

2.  Characterization of Mug33 reveals complementary roles for actin cable-dependent transport and exocyst regulators in fission yeast exocytosis.

Authors:  Hilary A Snaith; James Thompson; John R Yates; Kenneth E Sawin
Journal:  J Cell Sci       Date:  2011-06-07       Impact factor: 5.285

  2 in total

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