title: Purification and crystallization of the yeast elongation factor eEF2.
abstract: Crystals of the Saccharomyces cerevisiae elongation factor 2 (eEF2) in complex with GDP were obtained with the vapour-diffusion technique after rapid purification from industrial yeast. The crystals diffract to 2.85 A and belong to the space group P2(1)2(1)2(1). A yeast strain expressing a functional histidine-tagged eEF2 as the only form of the protein further allows facilitated purification of the factor for both structural and functional studies.
authors.affiliation: Institute of Molecular and Structural Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark.
authors.forename: René
authors.initials: R
authors.lastname: Jørgensen
authors.forename: Anne
authors.initials: A
authors.lastname: Carr-Schmid
authors.forename: Pedro A
authors.initials: PA
authors.lastname: Ortiz
authors.forename: Terri Goss
authors.initials: TG
authors.lastname: Kinzy
authors.forename: Gregers Rom
authors.initials: GR
authors.lastname: Andersen
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006639:Histidine / Q000737:chemistry; D009154:Mutation; D020652:Peptide Elongation Factor 2 / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000737:chemistry*
chemical_list: D020652:Peptide Elongation Factor 2; D006639:Histidine