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The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2007 Mar 01; Vol. 63 (Pt 3), pp. 209-13. Date of Electronic Publication: 2007 Feb 23. - Publication Year :
- 2007
-
Abstract
- Metal-binding sites are ubiquitous in proteins and can be readily utilized for phasing. It is shown that a protein crystal structure can be solved using single-wavelength anomalous diffraction based on the anomalous signal of a cobalt ion measured on a conventional monochromatic X-ray source. The unique absorption edge of cobalt (1.61 A) is compatible with the Cu K alpha wavelength (1.54 A) commonly available in macromolecular crystallography laboratories. This approach was applied to the determination of the structure of Melampsora lini avirulence protein AvrL567-A, a protein with a novel fold from the fungal pathogen flax rust that induces plant disease resistance in flax plants. This approach using cobalt ions may be applicable to all cobalt-binding proteins and may be advantageous when synchrotron radiation is not readily available.
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 63
- Issue :
- Pt 3
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 17329816
- Full Text :
- https://doi.org/10.1107/S1744309107004599