Crystallization of a hyperthermophilic archaeal elongation factor 1 alpha.
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.
Zagari
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A
Università di Napoli Federico II, Centro di Studio di Biocristallografia, CNR, Italy.
Sica
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Scarano
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Vitagliano
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L
Bocchini
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V
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*
D001426:Bacterial Proteins; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors