Scientists have mapped the first three-dimensional structure of a vault particle linked to bacterial life, uncovering a previously unexplored branch of these mysterious protein assemblies. The discovery could give researchers a simpler way to investigate structures found in human cells. Anthropic’s biology research team used Claude throughout the investigation, from identifying promising proteins to reconstructing their molecular architecture.

Vault particles have puzzled biologists for nearly four decades. Despite their enormous size and widespread presence in complex organisms, researchers still cannot explain their biological purpose. The new findings reveal that related proteins can assemble into similar structures in bacteria and bacteriophages. This discovery could help scientists trace their evolutionary history and understand their role in living cells.

Leonard Rome and Nancy Kedersha first identified vault particles in 1986. These hollow, barrel-shaped structures rank among the largest protein complexes found in human cells. Mammalian vaults contain 78 copies of a major protein arranged into two symmetrical halves.

Their biological purpose remains uncertain despite decades of investigation. Researchers have proposed roles in cellular transport, drug resistance, and immune defense. However, experiments have yet to establish any of these functions conclusively.

The structures also appear across much of the evolutionary tree. Their presence in organisms ranging from slime molds to humans suggests an important biological role. However, researchers have struggled to investigate them because common laboratory organisms lack vaults.

We’re sharing how our biology research team worked with Claude to map the first 3D structure of a vault particle from bacterial life. Vault particles are a longstanding mystery.

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