Crystallization of Bacteriophage fr and its Recombinant Capsids

Crystallization of Bacteriophage fr and its Recombinant Capsids

Single crystals of Escherichia coli bacteriophage fr and its recombinant capsids have been obtained by the vapour diffusion technique in the presence of ammonium sulphate. They diffract X-rays to at least 3·5 Å. Electron microscopic observation of the crystals revealed a three-dimensional lattice of...

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Veröffentlicht in:Journal of molecular biology 1993-08, Vol.232 (3), p.1005-1006
Hauptverfasser: Bundule, M., Pumpens, P., Ose, V., Valegård, K., Liljas, L.
Format: Artikel
Sprache:eng
Schlagworte:
Capsid - chemistry
Coliphages - chemistry
Crystallization
Escherichia coli
fr phage
phage fr
Protein Conformation
recombinant capsids
Recombinant Proteins - chemistry
X-ray studies
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Zusammenfassung:Single crystals of Escherichia coli bacteriophage fr and its recombinant capsids have been obtained by the vapour diffusion technique in the presence of ammonium sulphate. They diffract X-rays to at least 3·5 Å. Electron microscopic observation of the crystals revealed a three-dimensional lattice of particles with RNA phage morphology and dimensions.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1993.1451