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 3.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:05, 20 November 2007
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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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