Cloning, expression, and crystallization of a hyperthermophilic protein that is homologous to the eukaryotic translation initiation factor, eIF5A

Kyeong Kyu Kim, Hisao Yokota, Rosalind Kim, Sung Hou Kim

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

A gene coding for a protein homologous to a translation initiation factor of eukaryotes, eIF5A, was cloned from Methanococcus jannaschii, a hyperthermophile with an optimum growth temperature of 85 °C. The protein was overexpressed, purified and crystallized. The crystals were obtained by vapor diffusion method with 8% PEG 4000 as precipitant and belong to space group P4122 with unit cell dimensions a = b = 45.52 Å and c = 155.59 Å. These crystals diffract to at least 2.2 Å resolution.

Original languageEnglish
Pages (from-to)2268-2270
Number of pages3
JournalProtein Science
Volume6
Issue number10
DOIs
StatePublished - Oct 1997
Externally publishedYes

Keywords

  • Hyperthermophile
  • Methanococcus jannaschii
  • Translation initiation factor
  • X-ray crystallography

Fingerprint

Dive into the research topics of 'Cloning, expression, and crystallization of a hyperthermophilic protein that is homologous to the eukaryotic translation initiation factor, eIF5A'. Together they form a unique fingerprint.

Cite this