Scientists used cryo-electron microscopy (cryo-EM) to determine the structure of telomerase in the budding yeast Saccharomyces cerevisiae for the first time, thus gaining unprecedented insight into the functioning of this enzyme[2]. The structure of telomerase in yeast differs significantly from that in other eukaryotic organisms and consists of the RNA component TLC1, three Est proteins and the Pop1/6/7 complex, which form a compactly arranged core[2]. The enzyme also contains long RNA bonds that flexibly connect the γKu70/80 heterodimer and the Sm[2] heptamer. Scientists discovered that the Est3 protein acts as a "molecular glue" stabilizing the entire complex - when they disrupted its interactions with other components, telomeres began to shorten and the biological aging of cells was accelerated[2]. Est3 is a homologue of the human TPP1 protein, which is crucial for the recruitment of telomeres to telomerase and the regulation of its activity during DNA replication[2]. This study provides the first atomic view of the structure of the yeast telomerase holoenzyme and elucidates the mechanisms of its assembly and function[2].