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

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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.

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

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866054696091

Affiliations: Laboratory of Structural Biology, Life Sciences Building, Tsinghua University, Beijing, 100084, China;

Publication date: October 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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