Crystallization of the yeast elongation factor complex eEF1A–eEF1Bα

Crystals of the Saccharomyces cerevisiae elongation factor eEF1A (formerly EF-1α) in complex with a catalytic C-terminal fragment of the nucleotide-exchange factor eEF1Bα (formerly EF-1β) were grown by the sitting-drop vapour-diffusion technique, using polyethylene glycol 2000 monomethyl ether as precipitant. Crystals diffract to better than 1.7 Å and belong to the space group P2₁2₁2₁. The unit-cell parameters of the crystals are sensitive to the choice of cryoprotectant. The structure of the 61 kDa complex was determined with the multiple anomalous dispersion technique using three selenomethionine residues in a 11 kDa eEF1Bα fragment generated by limited proteolysis of full-length eEF1Bα expressed in Escherichia coli.