Ribosome biogenesis is one of the most intricate and energy-intensive processes in the cell. In our lab, we investigate how the large ribosomal subunit (60S) is assembled from RNA and proteins through a finely tuned series of enzymatic and structural events, mapping these processes at molecular resolution to reveal their order, timing, coordination, and regulation. Our focus is on the molecular machines, such as ATPases and GTPases, that drive these transitions, and on the quality-control mechanisms that ensure fidelity during assembly. Using cryo-electron microscopy, light microscopy, mass spectrometry, and integrative modeling, we visualize how these enzymes remodel RNA–protein complexes and drive conformational changes that couple pre-ribosomal maturation with its stepwise transport across multiple cellular compartments. By combining structural and biochemical approaches, we are building a detailed picture of how ribosome assembly is faithfully and efficiently executed within the cell.