2opc

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(New page: 200px<br /><applet load="2opc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2opc, resolution 1.43&Aring;" /> '''Structure of Melamps...)
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==Overview==
==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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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.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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 G, Wang CI, Forwood JK, Teh T, Catanzariti AM, Ellis JG, Dodds PN, Kobe B, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt, 3):209-13. Epub 2007 Feb 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17329816 17329816]
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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 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17329816 17329816]
[[Category: Melampsora lini]]
[[Category: Melampsora lini]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Catanzariti, A.M.]]
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[[Category: Catanzariti, A M.]]
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[[Category: Dodds, P.N.]]
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[[Category: Dodds, P N.]]
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[[Category: Ellis, J.G.]]
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[[Category: Ellis, J G.]]
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[[Category: Forwood, J.K.]]
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[[Category: Forwood, J K.]]
[[Category: Guncar, G.]]
[[Category: Guncar, G.]]
[[Category: Kobe, B.]]
[[Category: Kobe, B.]]
[[Category: Teh, T.]]
[[Category: Teh, T.]]
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[[Category: Wang, C.I.]]
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[[Category: Wang, C I.]]
[[Category: CO]]
[[Category: CO]]
[[Category: IMD]]
[[Category: IMD]]
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[[Category: single-wavelength anomalous dispersion (sad)]]
[[Category: single-wavelength anomalous dispersion (sad)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:32:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:02 2008''

Revision as of 16:21, 21 February 2008


2opc, resolution 1.43Å

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Structure of Melampsora lini avirulence protein, AvrL567-A

Overview

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.

About this Structure

2OPC is a Single protein structure of sequence from Melampsora lini with and as ligands. 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

Page seeded by OCA on Thu Feb 21 18:21:02 2008

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