Crystallization and Preliminary Crystallographic Analysis of Human Eukaryotic Translation Initiation Factor 5A (eIF-5A)

Title: Crystallization and Preliminary Crystallographic Analysis of Human Eukaryotic Translation Initiation Factor 5A (eIF-5A)

Volume: 12 Issue: 7

Author(s): Yuna Sun, Xuemei Li, Beili Wu, Ping Sun and Zihe Rao

Affiliation:

Keywords: Crystallographic Analysis, Human Eukaryotic Translation Initiation Factor 5A (eIF-5A), (NH4)2SO4, amino acid hypusine

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 291K using (NH4)2SO4 as precipitant. Diffraction data were obtained to a resolution of 2.7Å from a single frozen crystal belonging to space group C2, with unit-cell parameters a=147.1Å, b=60.4Å, c=76.4Å, β=92.4 . There are more than three molecules per asymmetric unit.

Cite this article as:

Sun Yuna, Li Xuemei, Wu Beili, Sun Ping and Rao Zihe, Crystallization and Preliminary Crystallographic Analysis of Human Eukaryotic Translation Initiation Factor 5A (eIF-5A), Protein & Peptide Letters 2005; 12 (7) . https://dx.doi.org/10.2174/0929866054696091

DOI https://dx.doi.org/10.2174/0929866054696091	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305