Cloning, expression, and crystallization of a hyperthermophilic protein that is homologous to the eukaryotic translation initiation factor, eIF5A.
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 degrees 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 P4(1)22 with unit cell dimensions a = b = 45.52 A and c = 155.59 A. These crystals diffract to at least 2.2 A resolution.
Kim
K K
KK
Structural Biology Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Yokota
H
H
Kim
R
R
Kim
S H
SH
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D017017:Methanococcus / Q000235:genetics*; D010448:Peptide Initiation Factors / Q000737:chemistry* / Q000235:genetics*; D016133:Polymerase Chain Reaction; D016601:RNA-Binding Proteins; D000097574:Eukaryotic Translation Initiation Factor 5A
D010448:Peptide Initiation Factors; D016601:RNA-Binding Proteins; D000097574:Eukaryotic Translation Initiation Factor 5A