Anthropic uses Claude to map prokaryotic vault

Anthropic's biology research lab reported the first 3D structure of a vault particle made in a prokaryotic cell. Claude was used at every stage of the project. The findings are in a preprint that has been submitted to bioRxiv but has not been posted yet.

Vaults are large, hollow protein barrels found in cells from slime molds to humans. Leonard Rome and Nancy Kedersha discovered them in 1986, and their function is still unknown. Related proteins had already been found in the genomes of prokaryotes and bacteriophages, but Anthropic says that, as far as it knows, nobody had shown before that these proteins assemble into complete vaults.

The team used cryo-electron microscopy to solve a vault built from a bacteriophage protein it calls L05. The particle contains 96 copies of the protein, 48 in each half, compared with 39 per half in mammalian vaults. It weighs about 9.5 megadaltons and is roughly 54 nanometers long and 45 wide, which makes it shorter and wider than the mammalian version. The researchers also made a larger vault by duplicating part of the protein. They suggest vaults like this could be adapted as nanocapsules for delivering enzymes.

Working under the team's direction, Claude searched protein databases, designed the DNA constructs, optimized the isolation method and processed the microscopy data. Anthropic says a purification that normally takes three days took about 90 minutes. A first structural model was ready 34 hours later, which the team estimates would normally have taken weeks.

The work does not explain what vaults do. Dr. Rome, who advised the team, said the breadth of the findings suggests "it is going to be a complicated function and an interesting ride." Anthropic says it will release the structures and more data soon.