The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein

Greg Guncar, Ching-I A. Wang, Jade Forwood, Trazel Teh, Ann-Maree. Catanzariti, Jeffrey G. Ellis, Peter N. Dodds, Bostjan Kobe

Research output: Contribution to journalArticle

8 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)209-213
Number of pages5
JournalActa Crystallographica Section F:Structural Biology Communications
Volume63
Issue number3
DOIs
Publication statusPublished - 2007

Fingerprint Dive into the research topics of 'The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein'. Together they form a unique fingerprint.

  • Cite this