The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29
is essential for viral DNA synthesis and is covalently bound to the
5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a
restriction endonuclease, the protein is bound to the two terminal
fragments. The 28,000 dalton protein can be visualized by electron
microscopy as a small dot and often is seen only when two ends are in
apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought
to improve the visibility of these small proteins by use of antibody
labeling.