Publication Abstract from PubMed
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.
The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.,Guncar G, Wang CI, Forwood JK, Teh T, Catanzariti AM, Ellis JG, Dodds PN, Kobe B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt, 3):209-13. Epub 2007 Feb 23. PMID:17329816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
