1cov
From Proteopedia
(New page: 200px<br /><applet load="1cov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cov, resolution 3.50Å" /> '''COXSACKIEVIRUS B3 CO...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1cov.gif|left|200px]]<br /><applet load="1cov" size=" | + | [[Image:1cov.gif|left|200px]]<br /><applet load="1cov" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cov, resolution 3.50Å" /> | caption="1cov, resolution 3.50Å" /> | ||
'''COXSACKIEVIRUS B3 COAT PROTEIN'''<br /> | '''COXSACKIEVIRUS B3 COAT PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of coxsackievirus B3 (CVB3) has been determined to | + | The crystal structure of coxsackievirus B3 (CVB3) has been determined to 3.5 A resolution. The icosahedral CVB3 particles crystallize in the monoclinic space group, P2(1), (a = 574.6, b = 302.1, c = 521.6 A, beta = 107.7 degrees ) with two virions in the asymmetric unit giving 120-fold non-crystallographic redundancy. The crystals diffracted to 2.7 A resolution and the X-ray data set was 55% complete to 3.0,4, resolution. Systematically weak reflections and the self-rotation function established pseudo R32 symmetry with each particle sitting on a 32 special position. This constrained the orientation and position of each particle in the monoclinic cell to near face-centered positions and allowed for a total of six possible monoclinic space-group settings. Correct interpretation of the high-resolution (3.0-3.2 A) self-rotation function was instrumental in determining the deviations from R32 orientations of the virus particles in the unit cell. Accurate particle orientations permitted the correct assignment of the crystal space-group setting amongst the six ambiguous possibilities and for the correct determination of particle positions. Real-space electron-density averaging and phase refinement, using human rhinovius 14 (HRV14) as an initial phasing model, have been carried out to 3.5 A resolution. The initial structural model has been built and refined to 3.5 A resolution using X-PLOR. |
==About this Structure== | ==About this Structure== | ||
| - | 1COV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_coxsackievirus_b1 Human coxsackievirus b1] with MYR and PLM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1COV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_coxsackievirus_b1 Human coxsackievirus b1] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=PLM:'>PLM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COV OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Human coxsackievirus b1]] | [[Category: Human coxsackievirus b1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Muckelbauer, J | + | [[Category: Muckelbauer, J K.]] |
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: MYR]] | [[Category: MYR]] | ||
[[Category: PLM]] | [[Category: PLM]] | ||
| Line 20: | Line 20: | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:10 2008'' |
Revision as of 10:08, 21 February 2008
|
COXSACKIEVIRUS B3 COAT PROTEIN
Overview
The crystal structure of coxsackievirus B3 (CVB3) has been determined to 3.5 A resolution. The icosahedral CVB3 particles crystallize in the monoclinic space group, P2(1), (a = 574.6, b = 302.1, c = 521.6 A, beta = 107.7 degrees ) with two virions in the asymmetric unit giving 120-fold non-crystallographic redundancy. The crystals diffracted to 2.7 A resolution and the X-ray data set was 55% complete to 3.0,4, resolution. Systematically weak reflections and the self-rotation function established pseudo R32 symmetry with each particle sitting on a 32 special position. This constrained the orientation and position of each particle in the monoclinic cell to near face-centered positions and allowed for a total of six possible monoclinic space-group settings. Correct interpretation of the high-resolution (3.0-3.2 A) self-rotation function was instrumental in determining the deviations from R32 orientations of the virus particles in the unit cell. Accurate particle orientations permitted the correct assignment of the crystal space-group setting amongst the six ambiguous possibilities and for the correct determination of particle positions. Real-space electron-density averaging and phase refinement, using human rhinovius 14 (HRV14) as an initial phasing model, have been carried out to 3.5 A resolution. The initial structural model has been built and refined to 3.5 A resolution using X-PLOR.
About this Structure
1COV is a Single protein structure of sequence from Human coxsackievirus b1 with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure determination of coxsackievirus B3 to 3.5 A resolution., Muckelbauer JK, Kremer M, Minor I, Tong L, Zlotnick A, Johnson JE, Rossmann MG, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):871-87. PMID:15299757
Page seeded by OCA on Thu Feb 21 12:08:10 2008
