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

Please use this identifier to cite or link to this item: https://doi.org/10.1107/S0907444903016123

Title:	Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2
Authors:	Wang, C.-H. Walsh, M. Balasubramanian, M.K. Dokland, T.
Issue Date:	1-Oct-2003
Citation:	Wang, C.-H., Walsh, M., Balasubramanian, M.K., Dokland, T. (2003-10-01). Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2. Acta Crystallographica - Section D Biological Crystallography 59 (10) : 1809-1812. ScholarBank@NUS Repository. https://doi.org/10.1107/S0907444903016123
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 P21. Br- and Hg-derivative data sets were measured to 2.21 Å 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.
Source Title:	Acta Crystallographica - Section D Biological Crystallography
URI:	http://scholarbank.nus.edu.sg/handle/10635/132775
ISSN:	09074449
DOI:	10.1107/S0907444903016123
Appears in Collections:	Staff Publications

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