The nucleotide-exchange factor isolated from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1b) consists of 90 residues and differs from eukaryal EF-1bs. The protein has been successfully crystallized using either microbatch-under-oil or vapour-diffusion methods. Crystals of native SsEF-1b diffract to 1.97 A° resolution and belong to space group P21212, 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-1b at 1.83 A° resolution. Model building using the phases derived from the MAD experiment is in progress
Crystallization and preliminary X-ray crystallographic analysis of the Sulfolobus solfataricus nucleotide exchange factor 1
RAIMO, Gennaro;
2005-01-01
Abstract
The nucleotide-exchange factor isolated from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1b) consists of 90 residues and differs from eukaryal EF-1bs. The protein has been successfully crystallized using either microbatch-under-oil or vapour-diffusion methods. Crystals of native SsEF-1b diffract to 1.97 A° resolution and belong to space group P21212, 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-1b at 1.83 A° resolution. Model building using the phases derived from the MAD experiment is in progressFile in questo prodotto:
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