title: Purification, crystallization and preliminary X-ray crystallographic analysis of mammalian translation elongation factor eEF1A2.
abstract: Translation elongation factor eEF1A2 was purified to homogeneity from rabbit muscle by two consecutive ion-exchange column-chromatography steps and this mammalian eEF1A2 was successfully crystallized for the first time. Protein crystals obtained using ammonium sulfate as precipitant diffracted to 2.5 Å resolution and belonged to space group P6(1)22 or P6(3)22 (unit-cell parameters a = b = 135.4, c = 304.6 Å). A complete native data set was collected to 2.7 Å resolution.
authors.affiliation: State Key Laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, 150 Zabolotnogo Street, 03680 Kyiv-143, Ukraine.
authors.forename: A
authors.initials: A
authors.lastname: Yaremchuk
authors.forename: V F
authors.initials: VF
authors.lastname: Shalak
authors.forename: O V
authors.initials: OV
authors.lastname: Novosylna
authors.forename: B S
authors.initials: BS
authors.lastname: Negrutskii
authors.forename: T
authors.initials: T
authors.lastname: Crépin
authors.forename: A V
authors.initials: AV
authors.lastname: El'skaya
authors.forename: M
authors.initials: M
authors.lastname: Tukalo
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D020648:Peptide Elongation Factor 1 / Q000737:chemistry* / Q000302:isolation & purification; D011817:Rabbits
chemical_list: D020648:Peptide Elongation Factor 1