1ev1
From Proteopedia
(New page: 200px<br /><applet load="1ev1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ev1, resolution 3.55Å" /> '''ECHOVIRUS 1'''<br />...) |
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| - | [[Image:1ev1.jpg|left|200px]]<br /><applet load="1ev1" size=" | + | [[Image:1ev1.jpg|left|200px]]<br /><applet load="1ev1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ev1, resolution 3.55Å" /> | caption="1ev1, resolution 3.55Å" /> | ||
'''ECHOVIRUS 1'''<br /> | '''ECHOVIRUS 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The atomic structure of echovirus 1 (a member of the enterovirus genus of | + | The atomic structure of echovirus 1 (a member of the enterovirus genus of the picornavirus family) has been determined using cryo-crystallography and refined to 3.55 A resolution. Echovirus 1 crystallizes in space group P22121 with a = 352.45, b = 472.15 and c = 483.20 A. The crystals contain one full virus particle in the asymmetric unit allowing for 60-fold noncrystallographic symmetry averaging. The diffraction pattern shows strong pseudo-B-centering with reflections with h + l = 2n + 1 being systematically weak or absent below about 6 A resolution. The size of the unit cell and presence of pseudo-B-centering placed strong constraints on the allowed packing of the icosahedral particle in the crystal lattice. These constraints greatly facilitated the determination of the orientation and position of the virus by reducing the dimensionality of the search, but interactions between the crystallographic and noncrystallographic symmetries rendered the choice of space group ambiguous until very late in the structure determination. This structure determination provides a striking example of the power of packing analysis in molecular replacement and illustrates how subtle interactions between crystallographic and noncrystallographic symmetries can be resolved. |
==About this Structure== | ==About this Structure== | ||
| - | 1EV1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_echovirus_11 Human echovirus 11] with MYR and PLM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1EV1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_echovirus_11 Human echovirus 11] 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=1EV1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human echovirus 11]] | [[Category: Human echovirus 11]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Filman, D | + | [[Category: Filman, D J.]] |
| - | [[Category: Hogle, J | + | [[Category: Hogle, J M.]] |
| - | [[Category: Wien, M | + | [[Category: Wien, M W.]] |
[[Category: MYR]] | [[Category: MYR]] | ||
[[Category: PLM]] | [[Category: PLM]] | ||
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[[Category: viral coat protein]] | [[Category: viral coat protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:48 2008'' |
Revision as of 10:31, 21 February 2008
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ECHOVIRUS 1
Overview
The atomic structure of echovirus 1 (a member of the enterovirus genus of the picornavirus family) has been determined using cryo-crystallography and refined to 3.55 A resolution. Echovirus 1 crystallizes in space group P22121 with a = 352.45, b = 472.15 and c = 483.20 A. The crystals contain one full virus particle in the asymmetric unit allowing for 60-fold noncrystallographic symmetry averaging. The diffraction pattern shows strong pseudo-B-centering with reflections with h + l = 2n + 1 being systematically weak or absent below about 6 A resolution. The size of the unit cell and presence of pseudo-B-centering placed strong constraints on the allowed packing of the icosahedral particle in the crystal lattice. These constraints greatly facilitated the determination of the orientation and position of the virus by reducing the dimensionality of the search, but interactions between the crystallographic and noncrystallographic symmetries rendered the choice of space group ambiguous until very late in the structure determination. This structure determination provides a striking example of the power of packing analysis in molecular replacement and illustrates how subtle interactions between crystallographic and noncrystallographic symmetries can be resolved.
About this Structure
1EV1 is a Protein complex structure of sequences from Human echovirus 11 with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure determination of echovirus 1., Filman DJ, Wien MW, Cunningham JA, Bergelson JM, Hogle JM, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1261-72. PMID:10089503
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