Crystallization and preliminary X-ray crystallographic analysis of the Sulfolobus solfataricus nucleotide-exchange factor 1beta.
The nucleotide-exchange factor isolated from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1beta) consists of 90 residues and differs from eukaryal EF-1betas. The protein has been successfully crystallized using either microbatch-under-oil or vapour-diffusion methods. Crystals of native SsEF-1beta diffract to 1.97 A resolution and belong to space group P2(1)2(1)2, with unit-cell parameters a = 106.46, b = 54.87, c = 44.03 A. Diffraction data have also been collected from a selenomethionine derivative of SsEF-1beta at 1.83 A resolution. Model building using the phases derived from the MAD experiment is in progress.
Ruggiero
Alessia
A
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Naples, Italy.
Masullo
Mariorosario
M
Arcari
Paolo
P
Raimo
Gennaro
G
Vitagliano
Luigi
L
Zagari
Adriana
A
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D020662:Guanine Nucleotide Exchange Factors / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012645:Selenomethionine / Q000737:chemistry; D013329:Structure-Activity Relationship; D048229:Sulfolobus solfataricus / Q000378:metabolism*; D014961:X-Ray Diffraction
D020662:Guanine Nucleotide Exchange Factors; D011994:Recombinant Proteins; D012645:Selenomethionine