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There is a need for improved tools for labeling protein species within large macromolecular assemblies. Here we describe a method for the efficient selenomethionine labeling of the membrane-containing bacterial virus PM2 for structural studies. By examining potential host cells a strain was found which was auxotrophic for methionine, and by performing a multiparameter search of conditions it was possible to derive a robust protocol which simultaneously minimized the toxic effects of the selenomethionine, so that a reasonable virus yield was maintained, whilst still achieving essentially complete labeling. This has allowed us to fingerprint the protein constituents of the virus in a relatively low resolution electron density map. Such a technique can be adapted to other macromolecule complexes studied by X-ray crystallography.

Original publication




Journal article


J Struct Biol

Publication Date





204 - 210


Corticoviridae, Crystallography, X-Ray, Methods, Selenomethionine