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

rust fungi
Flax
Crystallization
Cobalt
X-Rays
crystallization
proteins
X rays
cobalt
Proteins
x rays
Ions
Plant Diseases
plant diseases
Wavelength
Crystallography
Synchrotrons
Disease Resistance
Pathogens
Synchrotron radiation

Cite this

Guncar, Greg ; Wang, Ching-I A. ; Forwood, Jade ; Teh, Trazel ; Catanzariti, Ann-Maree. ; Ellis, Jeffrey G. ; Dodds, Peter N. ; Kobe, Bostjan. / The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein. In: Acta Crystallographica Section F:Structural Biology Communications. 2007 ; Vol. 63, No. 3. pp. 209-213.
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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.",
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The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein. / Guncar, Greg; Wang, Ching-I A.; Forwood, Jade; Teh, Trazel; Catanzariti, Ann-Maree.; Ellis, Jeffrey G.; Dodds, Peter N.; Kobe, Bostjan.

In: Acta Crystallographica Section F:Structural Biology Communications, Vol. 63, No. 3, 2007, p. 209-213.

Research output: Contribution to journalArticle

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AU - Guncar, Greg

AU - Wang, Ching-I A.

AU - Forwood, Jade

AU - Teh, Trazel

AU - Catanzariti, Ann-Maree.

AU - Ellis, Jeffrey G.

AU - Dodds, Peter N.

AU - Kobe, Bostjan

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AB - 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.

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