Crystallization and preliminary X-ray diffraction studies of DNA polymerase from the thermophilic archaeon Sulfolobus solfataricus.
The thermophilic and thermostable family B DNA polymerase from the archaeon Sulfolobus solfataricus (Mr of about 100 kDa) has been crystallized by the hanging-drop vapour-diffusion method at 294 K using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group C2 with cell dimensions a = 187.4, b = 68.5, c = 125.8 A and beta = 107.8 degrees and diffract up to 2.7 A resolution on a rotating-anode X-ray source. Native data have been collected at 100 K. A heavy-atom derivative search is in progress.
Nastopoulos
V
V
Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Università di Roma 'La Sapienza', P. le A. Moro, 5, 00185 Rome, Italy.
Pisani
F M
FM
Savino
C
C
Federici
L
L
Rossi
M
M
Tsernoglou
D
D
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D016944:Sulfolobus / Q000201:enzymology*
D001426:Bacterial Proteins; D004259:DNA-Directed DNA Polymerase