Researchers used Claude to investigate vaults, large hollow protein shells found across eukaryotes whose biological function remains unknown. Although related proteins had been identified in bacteria and bacteriophages, it was unclear whether they formed complete vaults. By searching a database of about 15 billion predicted proteins, the team found rare vault-protein relatives across 29 bacterial and four archaeal groups. They tested selected candidates and identified a bacteriophage protein, L05, that assembles into a vault inside bacteria. This offers a simpler system for studying vault origins and structure, but does not yet explain what vaults do.
Cryo-electron microscopy revealed that the L05 vault contains 96 protein copies, weighs about 9.5 megadaltons, and is shorter, wider, and more spherical than the mammalian version. Experiments with 15 altered proteins showed that changes near the caps can prevent the shell from closing, while adding two repeated wall segments produces a larger vault with about 20% more internal volume. Claude contributed to sequence searches, DNA design, isolation-method development, and microscopy analysis. A new chromatography method reduced purification from roughly three days to 90 minutes, and the first structural model was ready 34 hours later - work estimated to take weeks by conventional methods. The findings illuminate how vaults assemble and may support engineered nanocapsules for enzyme delivery, while leaving their natural role unresolved.
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