Preliminary structural investigations of the Eut‐L shell protein of the ethanolamine ammonia‐lyase metabolosome of Escherichia coli
The ethanolamine ammonia‐lyase microcompartment is composed of five different shell proteins that have been proposed to assemble into symmetrically shaped polyhedral particles of varying sizes. Here, preliminary X‐ray analysis of crystals of the bacterial microcompartment shell protein Eut‐L from Escherichia coli is reported. Cloning, overexpression and purification resulted in highly pure protein that crystallized readily under many different conditions. In all cases the protein forms thin hexagonal plate‐shaped crystals belonging to space group P3 that are of unusually high stability against different solvent conditions. The crystals diffracted to a resolution of 2.0 Å using synchrotron radiation but proved to be radiation‐sensitive. Preparations of heavy‐atom‐derivatized crystals for use in determining the three‐dimensional structure are under way.
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