2opc: Difference between revisions

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[[Image:2opc.gif|left|200px]]
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{{STRUCTURE_2opc|  PDB=2opc  |  SCENE=  }}  
{{STRUCTURE_2opc|  PDB=2opc  |  SCENE=  }}  


'''Structure of Melampsora lini avirulence protein, AvrL567-A'''
===Structure of Melampsora lini avirulence protein, AvrL567-A===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17329816}}


==About this Structure==
==About this Structure==
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[[Category: Crystallization]]
[[Category: Crystallization]]
[[Category: Plant disease resistance]]
[[Category: Plant disease resistance]]
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Revision as of 23:04, 27 July 2008

File:2opc.png

Template:STRUCTURE 2opc

Structure of Melampsora lini avirulence protein, AvrL567-A

Template:ABSTRACT PUBMED 17329816

About this Structure

2OPC is a Single protein structure of sequence from Melampsora lini. Full crystallographic information is available from OCA.

Reference

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

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