Analysis of the single-stranded DNA bacteriophage phi X174, refined at a resolution of 3.0 A.

@article{McKenna1994AnalysisOT,
  title={Analysis of the single-stranded DNA bacteriophage phi X174, refined at a resolution of 3.0 A.},
  author={Robert McKenna and Leopold L Ilag and Michael G. Rossmann},
  journal={Journal of molecular biology},
  year={1994},
  volume={237 5},
  pages={517-43}
}
The structure of the bacteriophage phi X174 was examined in a 2.7 A resolution map and refined, using 6.0 A to 3.0 A resolution data with F > or = 5 sigma (F). The final R-factor was 20.9% and the root-mean-square deviation from idealized bond lengths was 0.021 A. The Hendrickson-Konnert refinement was restrained by the phases derived from the molecular replacement icosahedral averaging procedure. The mature phage capsid consists of 60 copies of the F protein with 426 amino acids, the G protein… CONTINUE READING
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