Open AccessThe use of Co 2+ for crystallization and structure determination, using a conventional monochromatic X‐ray source, of flax rust avirulence protein
Author(s) -
Gunčar Gregor,
Wang ChingI A.,
Forwood Jade K.,
Teh Trazel,
Catanzariti AnnMaree,
Ellis Jeffrey G.,
Dodds Peter N.,
Kobe Boštjan
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107004599
Subject(s) - cobalt , protein crystallization , monochromatic color , crystallization , crystallography , diffraction , anomalous scattering , synchrotron , crystal structure , materials science , phaser , synchrotron radiation , chemistry , optics , physics , inorganic chemistry , organic chemistry
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 Å) is compatible with the Cu K α wavelength (1.54 Å) 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.