1frs

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(New page: 200px<br /><applet load="1frs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frs, resolution 3.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1frs.gif|left|200px]]<br /><applet load="1frs" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1frs, resolution 3.5&Aring;" />
caption="1frs, resolution 3.5&Aring;" />
'''CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The structure of recombinant capsids of the bacterial virus fr has been, determined by X-ray crystallography at 3.5 A resolution. The capsids were, produced by expressing the fr coat protein in Escherichia coli, the, natural host of the virus, and are probably essentially identical to the, protein shell of the native virus. The structure was determined using, molecular replacement with the protein shell of the related MS2 virus, and, refined to a crystallographic R-factor of 0.228. A comparison of the, protein shells of the viruses shows that they are very similar, and, indicates that they may have a similar regulation of the assembly of the, quasi-symmetrical protein shell.
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The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 A resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.
==About this Structure==
==About this Structure==
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1FRS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_fr Enterobacteria phage fr]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRS OCA].
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1FRS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_fr Enterobacteria phage fr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRS OCA].
==Reference==
==Reference==
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[[Category: icosahedral virus]]
[[Category: icosahedral virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:12:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:59 2008''

Revision as of 10:42, 21 February 2008


1frs, resolution 3.5Å

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CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION

Overview

The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 A resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.

About this Structure

1FRS is a Single protein structure of sequence from Enterobacteria phage fr. Full crystallographic information is available from OCA.

Reference

Crystal structure of bacteriophage fr capsids at 3.5 A resolution., Liljas L, Fridborg K, Valegard K, Bundule M, Pumpens P, J Mol Biol. 1994 Dec 2;244(3):279-90. PMID:7966339

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