Crystallization of the yeast elongation factor complex eEF1A-eEF1B alpha

Crystals of the Saccharomyces cerevisiae elongation factor eEF1A (formerly EF-1 alpha) in complex with a catalytic C-terminal fragment of the nucleoti de-exchange factor eEF1B alpha (formerly EF-1 beta) were grown by the sitti ng-drop vapour-diffusion technique, using polyethylene glycol 2000 monometh yl ether as precipitant. Crystals diffract to better than 1.7 Angstrom and belong to the space group P2(1)2(1)2(1). The unit-cell parameters of the cr ystals are sensitive to the choice of cryoprotectant. The structure of the 61 kDa complex was determined with the multiple anomalous dispersion techni que using three selenomethionine residues in a 11 kDa eEF1B alpha fragment generated by limited proteolysis of full-length eEF1B alpha expressed in Es cherichia coli.