Reference - PMID:14501122 - Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2.
Reference summary
- PubMed ID
- PMID:14501122
- Title
- Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2.
- Authors
- Wang CH, Walsh M, Balasubramanian MK, Dokland T
- Citation
- Acta Crystallogr D Biol Crystallogr 2003 Oct;59(Pt 10):1809-12
- Publication year
- 2003
- 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.
