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Anthropic maps first prokaryotic vault with Claude

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Anthropic’s biology lab used Claude to solve the first 3D structure of a vault built from prokaryotic/phage protein. Purification takes about 90 minutes; a preprint is on bioRxiv.

· 1 min read

Cryo-EM style graphic of a vault protein particle from Anthropic research
Image: Anthropic · Press kit · Source

What they found

Anthropic’s Science team reported the first 3D structure of a vault particle assembled from prokaryotic and bacteriophage MVP homologs. Vaults have been known in eukaryotes since 1986; their function is still unconfirmed. The project sits alongside other AI-accelerated wet-lab efforts such as Intology Locus, with Claude embedded across search, construct design, isolation, and cryo-EM processing.

Numbers and method

  • Phage protein L05: 96 copies, ~9.5 megadaltons, ~54×45 nm, ~25% more internal volume than human vaults.
  • Screened ~15 billion proteins; MVP homologs in 29 bacterial and 4 archaeal phyla, under 1% of species.
  • Size-exclusion chromatography cut purification to ~90 minutes versus multi-day sucrose gradients.
  • First full cryo-EM model in 34 hours; the team documented its own failures, including a two-week protocol error and a mirrored map.

Limits

Particles have only been produced in E. coli so far, not yet shown in native bacterial or phage hosts. Function remains open. A preprint was submitted to bioRxiv; structures and extra data are promised later.

    By Mikola Máté Patrik

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