Please use this identifier to cite or link to this item:
|Title:||Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2|
|Source:||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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 9, 2018
WEB OF SCIENCETM
checked on Nov 29, 2017
checked on Jan 15, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.