Assemblage of structural proteins into 50S subunits was examined in Escherichia coli recovering from chloramphenicol treatment. Cells previously labeled with H3-leucine for three generations were incubated for 30 minutes with chloramphenicol. Proteins synthesized during the initial 5 minutes of recovery from chloramphenicol treatment were labeled with C13-leucine. Marked variation in the ratios of C14 to H3-leucine in ribosomal protein occurred in cells that had been treated with chloramphenicol; untreated cells displayed little variation. The results suggest that ribosomal proteins are assembled into 50S subunits in a nonrandom manner.