Making Complexes Simply

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Science  30 Mar 2007:
Vol. 315, Issue 5820, pp. 1768
DOI: 10.1126/science.315.5820.1768c

Even though proteomic studies may overestimate the number and variety of functionally important protein-protein interactions in cells, most such complexes are not abundant enough to be purified via classical biochemistry. Heterologous expression of well-folded proteins in the milligram amounts needed for structural studies is not straightforward—especially not for posttranslationally modified eukaryotic proteins—and arranging stoichiometric assembly is yet another hurdle.

Fitzgerald et al. describe a baculovirus-based system for making multigene expression vectors and demonstrate its utility for producing in parallel a combinatorial set of chromatinremodeling complexes built of wild-type or truncated subunits. Incorporating a phosphatase into the expression vector quantitatively yielded the de-phospho form of the complex. — GJC

Structure 15, 275 (2007).

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