Purification and crystallization of the yeast elongation factor eEF2

Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):712-5. doi: 10.1107/s0907444902003001. Epub 2002 Mar 22.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Histidine / chemistry
  • Mutation
  • Peptide Elongation Factor 2 / chemistry*
  • Peptide Elongation Factor 2 / genetics
  • Peptide Elongation Factor 2 / isolation & purification
  • Saccharomyces cerevisiae / chemistry*

Substances

  • Peptide Elongation Factor 2
  • Histidine