Table - link
||Choi KH et al., Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4. J Mol Biol. 2008 May 2 378(3):726-36. doi: 10.1016/j.jmb.2008.02.059. p.727 table 1PubMed ID18374942
||Falco, S. C., Zehring, W. & Rothman-Denes, L. B. (1980). DNA-dependent RNA polymerase from bacteriophage N4 virions. Purification and characterization. J. Biol. Chem. 255, 4339–4347.PubMed ID6989837
||Primary source abstract: "A DNA-dependent RNA polymerase has been purified to homogeneity from bacteriophage N4 virions. Sodium dodecyl sulfate-8 M urea polyacrylamide gel electrophoresis of the enzyme revealed a single polypeptide with a molecular weight of 350,000. The hydrodynamic properties of the enzyme have been determined to be 9.5 S for the sedimentation coefficient and 84 A for the Stokes radius."
||P.727 left column bottom paragraph: "The isometric head of N4 has a diameter of approximately 700 Å. A short, non-contractile tail is attached to the head [ref 15] The mature virion contains at least 10 gene products (gp) (Table 1) [primary source]. gp50, the
vRNAP [DNA-dependent RNA
polymerase], consists of 3500 amino acids and is present in the virion [primary source]."