Purification, Properties and Assembly of the Neck‐Appendage Protein of the Bacillus subtilis Phage φ 29

Abstract
The purification of the neck appendage protein of .vphi.29,p12*, which is involved in the adsorption of the phage to B. subtilis, is described. The purified native protein is in a dimeric form and can be assembled, in vitro, onto purified 12- particles that lack the neck appendages, suggesting that the incorporation of p12* to the rest of the phage structure is a self-assembly process. The assembly of protein p12* in vitro follows cooperative kinetics and it occurs with an efficiency of about 4%.