title: Crystallization and preliminary crystallographic analysis of human eukaryotic translation initiation factor 5A (eIF-5A).
abstract: Eukaryotic translation initiation factor 5A (eIF-5A) is universally found in all eukaryotic cells. It is the only protein in nature known to contain the unusual amino acid hypusine, a post-translationally modified lysine. Recombinant human eIF-5A was crystallized by the hanging-drop vapor diffusion method. Crystals were grown at 291 K using (NH4)2SO4 as precipitant. Diffraction data were obtained to a resolution of 2.7 A from a single frozen crystal belonging to space group C2, with unit-cell parameters a = 147.1 A, b = 60.4 A, c = 76.4 A, beta = 92.4 degrees. There are more than three molecules per asymmetric unit.
authors.affiliation: Laboratory of Structural Biology, Life Sciences Building, Tsinghua University, Beijing, 100084, China.
authors.forename: Yuna
authors.initials: Y
authors.lastname: Sun
authors.forename: Xuemei
authors.initials: X
authors.lastname: Li
authors.forename: Beili
authors.initials: B
authors.lastname: Wu
authors.forename: Ping
authors.initials: P
authors.lastname: Sun
authors.forename: Zihe
authors.initials: Z
authors.lastname: Rao
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D010448:Peptide Initiation Factors / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry*; D000097574:Eukaryotic Translation Initiation Factor 5A
chemical_list: D010448:Peptide Initiation Factors; D016601:RNA-Binding Proteins; D000097574:Eukaryotic Translation Initiation Factor 5A