title: Crystallization of a hyperthermophilic archaeal elongation factor 1 alpha.
abstract: Intact and fully active elongation factor aEF-1 alpha from the hyperthermophilic archaeon Sulfolobus solfataricus has been crystallized as a complex with GDP. Crystals were stable at temperatures below 8 degrees C and showed significant diffraction beyond 3.0 A. The orthorhombic lattice parameters were a = 62.9 A, b = 81.3 A, c = 115.6 A with one molecule per asymmetric unit.
authors.affiliation: Università di Napoli Federico II, Centro di Studio di Biocristallografia, CNR, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Zagari
authors.forename: F
authors.initials: F
authors.lastname: Sica
authors.forename: G
authors.initials: G
authors.lastname: Scarano
authors.forename: L
authors.initials: L
authors.lastname: Vitagliano
authors.forename: V
authors.initials: V
authors.lastname: Bocchini
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000737:chemistry*; D016944:Sulfolobus / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors