Published in
International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 3(63), p. 209-213, 2007
DOI: 10.1107/s1744309107004599
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- ORCID
- International Union of Crystallography
- [www.ncbi.nlm.nih.gov] | PDF
- [espace.library.uq.edu.au]
- [europepmc.org] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [espace.library.uq.edu.au] | PDF
- [www.researchgate.net] | PDF
Tools
The use of Co2+for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein
,
Trazel Teh,
Ann-Maree Catanzariti,
Jeffrey G. Ellis,
Peter N. Dodds,
Boštjan Kobe
Full text: Download
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 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.