1anv
From Proteopedia
(New page: 200px<br /><applet load="1anv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1anv, resolution 2.7Å" /> '''ADENOVIRUS 5 DBP/URAN...) |
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| - | [[Image:1anv.gif|left|200px]]<br /><applet load="1anv" size=" | + | [[Image:1anv.gif|left|200px]]<br /><applet load="1anv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1anv, resolution 2.7Å" /> | caption="1anv, resolution 2.7Å" /> | ||
'''ADENOVIRUS 5 DBP/URANYL FLUORIDE SOAK'''<br /> | '''ADENOVIRUS 5 DBP/URANYL FLUORIDE SOAK'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Soaking crystals of the C-terminal DNA-binding domain of the adenovirus | + | Soaking crystals of the C-terminal DNA-binding domain of the adenovirus single-stranded DNA-binding protein with a buffer containing K(3)UO(2)F(5) results in a 9% change of the crystallographic c axis without destruction of the crystals or appreciable loss of resolution. The crystals belong to space group P2(1)2(1)2(1) with a = 79.7, b = 75.6 and c = 60.6 A. The three-dimensional structure has been refined to 2.7 A with a crystallographic R factor of 0.206. Antiparallel chains of protein molecules running through the entire crystal are linked by uranyl ions. The relative orientation of protein monomers is flexible, even in the crystalline state, and allows changes in the packing of the protein chains. |
==About this Structure== | ==About this Structure== | ||
| - | 1ANV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_11 Human adenovirus 11] with ZN and IUM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ANV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_11 Human adenovirus 11] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=IUM:'>IUM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human adenovirus 11]] | [[Category: Human adenovirus 11]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kanellopoulos, P | + | [[Category: Kanellopoulos, P N.]] |
[[Category: Tsernoglou, D.]] | [[Category: Tsernoglou, D.]] | ||
| - | [[Category: Tucker, P | + | [[Category: Tucker, P A.]] |
| - | [[Category: Vliet, P | + | [[Category: Vliet, P C.Van Der.]] |
[[Category: IUM]] | [[Category: IUM]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:30 2008'' |
Revision as of 09:46, 21 February 2008
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ADENOVIRUS 5 DBP/URANYL FLUORIDE SOAK
Overview
Soaking crystals of the C-terminal DNA-binding domain of the adenovirus single-stranded DNA-binding protein with a buffer containing K(3)UO(2)F(5) results in a 9% change of the crystallographic c axis without destruction of the crystals or appreciable loss of resolution. The crystals belong to space group P2(1)2(1)2(1) with a = 79.7, b = 75.6 and c = 60.6 A. The three-dimensional structure has been refined to 2.7 A with a crystallographic R factor of 0.206. Antiparallel chains of protein molecules running through the entire crystal are linked by uranyl ions. The relative orientation of protein monomers is flexible, even in the crystalline state, and allows changes in the packing of the protein chains.
About this Structure
1ANV is a Single protein structure of sequence from Human adenovirus 11 with and as ligands. Full crystallographic information is available from OCA.
Reference
Conformational change of the adenovirus DNA-binding protein induced by soaking crystals with K3UO2F5 solutions., Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA, Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):942-5. PMID:15299602
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