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 angstrom) is compatible with the Cu K alpha wavelength (1.54 angstrom) 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.
|Number of pages||5|
|Journal||Acta Crystallographica Section F:Structural Biology Communications|
|Publication status||Published - 2007|
Guncar, G., Wang, C-I. A., Forwood, J., Teh, T., Catanzariti, A-M., Ellis, J. G., Dodds, P. N., & Kobe, B. (2007). The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein. Acta Crystallographica Section F:Structural Biology Communications, 63(3), 209-213. https://doi.org/10.1107/S1744309107004599