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Purification, crystallization, small-angle X-ray scattering and preliminary X-ray diffraction analysis of the SH2 domain of the Csk-homologous kinase.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Mar2011, Vol. 67 Issue 3, p336-339. 4p. - Publication Year :
- 2011
-
Abstract
- The C-terminal Src kinase (Csk) and Csk-homologous kinase (CHK) are endogenous inhibitors of the proto-oncogenic Src family of protein tyrosine kinases (SFKs). Phosphotyrosyl peptide binding to their Src-homology 2 (SH2) domains activates Csk and CHK, enhancing their ability to suppress SFK signalling; however, the detailed mechanistic basis of this activation event is unclear. The CHK SH2 was expressed in Escherichia coli and the purified protein was characterized as monomeric by synchrotron small-angle X-ray scattering in-line with size-exclusion chromatography. The CHK SH2 crystallized in 0.2 M sodium bromide, 0.1 M bis-Tris propane pH 6.5 and 20% polyethylene glycol 3350 and the best crystals diffracted to ∼1.6 Å resolution. The crystals belonged to space group P2, with unit-cell parameters a = 25.8, b = 34.6, c = 63.2 Å, β = 99.4°. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 67
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812711
- Full Text :
- https://doi.org/10.1107/S1744309110053728