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Title: Crystallization and preliminary X-ray crystallographic analysis of the Sulfolobus solfataricus nucleotide-exchange factor 1β

Journal Article · · Acta Crystallographica. Section F
 [1];  [2];  [3];  [3];  [1];  [1]
  1. Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Napoli (Italy)
  2. Dipartimento di Scienze Farmacobiologiche, Università degli Studi Magna Graecia, Roccelletta di Borgia, I-88021 Catanzaro (Italy)
  3. Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi Federico II, I-80131 Napoli (Italy)

Nucleotide-exchange factor from S. solfataricus (SsEF-1β) has been successfully crystallized. X-ray diffraction data have been collected from the native enzyme and from the selenomethionine derivative of SsEF-1β to 1.97 and 1.83 Å resolution, respectively. The nucleotide-exchange factor isolated from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1β) consists of 90 residues and differs from eukaryal EF-1βs. The protein has been successfully crystallized using either microbatch-under-oil or vapour-diffusion methods. Crystals of native SsEF-1β diffract to 1.97 Å resolution and belong to space group P2{sub 1}2{sub 1}2, with unit-cell parameters a = 106.46, b = 54.87, c = 44.03 Å. Diffraction data have also been collected from a selenomethionine derivative of SsEF-1β at 1.83 Å resolution. Model building using the phases derived from the MAD experiment is in progress.

OSTI ID:
22356186
Journal Information:
Acta Crystallographica. Section F, Vol. 61, Issue Pt 11; Other Information: PMCID: PMC1978138; PMID: 16511218; PUBLISHER-ID: bw5106; OAI: oai:pubmedcentral.nih.gov:1978138; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English