Thioltransferase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique protein disulfide oxidoreductase. The recombinant protein expressed in Escherichia coli was crystallized by the sitting drop vapor diffusion method, using polyethylene glycol 550 monomethyl ether as the precipitant. The crystals belong to the hexagonal space group P6122 or P6522, with unit cell dimensions of a 5 b 5 110.6 Å and c 5 68.4 Å and with one monomer in the asymmetric unit. The crystals diffracted beyond 2.0 Å and a complete native data set was collected to 2.3 Å resolution. The solution of the crystal structure by multiple isomorphous replacement is in progress.
Crystallization and Preliminary X-ray Structure Analysis of a Hyperthermostable Thioltransferase from the Archaeon Pyrococcus furiosus / Ren, B.; Tibbelin, G.; Rossi, M.; Bartolucci, Simonetta; Ladenstein, R.. - In: JOURNAL OF STRUCTURAL BIOLOGY. - ISSN 1047-8477. - STAMPA. - 119:1(1997), pp. 1-5. [10.1006/jsbi.1997.3870]
Crystallization and Preliminary X-ray Structure Analysis of a Hyperthermostable Thioltransferase from the Archaeon Pyrococcus furiosus.
BARTOLUCCI, SIMONETTA;
1997
Abstract
Thioltransferase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique protein disulfide oxidoreductase. The recombinant protein expressed in Escherichia coli was crystallized by the sitting drop vapor diffusion method, using polyethylene glycol 550 monomethyl ether as the precipitant. The crystals belong to the hexagonal space group P6122 or P6522, with unit cell dimensions of a 5 b 5 110.6 Å and c 5 68.4 Å and with one monomer in the asymmetric unit. The crystals diffracted beyond 2.0 Å and a complete native data set was collected to 2.3 Å resolution. The solution of the crystal structure by multiple isomorphous replacement is in progress.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
