Crystallization and preliminary crystallographic analysis of human eukaryotic translation initiation factor 5A (eIF-5A)

Protein Pept Lett. 2005 Oct;12(7):713-5. doi: 10.2174/0929866054696091.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Eukaryotic Translation Initiation Factor 5A
  • Humans
  • Peptide Initiation Factors / chemistry*
  • RNA-Binding Proteins / chemistry*

Substances

  • Peptide Initiation Factors
  • RNA-Binding Proteins