Crystallization and preliminary X-ray diffraction studies of DNA polymerase from the thermophilic archaeon Sulfolobus solfataricus

V Nastopoulos; F M Pisani; C Savino; L Federici; M Rossi; D Tsernoglou

doi:10.1107/s0907444998002443

Crystallization and preliminary X-ray diffraction studies of DNA polymerase from the thermophilic archaeon Sulfolobus solfataricus

Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1002-4. doi: 10.1107/s0907444998002443.

Authors

V Nastopoulos¹, F M Pisani, C Savino, L Federici, M Rossi, D Tsernoglou

Affiliation

¹ Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Università di Roma 'La Sapienza', P. le A. Moro, 5, 00185 Rome, Italy.

PMID: 9757120
DOI: 10.1107/s0907444998002443

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / isolation & purification
Crystallization
Crystallography, X-Ray
DNA-Directed DNA Polymerase / chemistry*
DNA-Directed DNA Polymerase / isolation & purification
Protein Conformation*
Sulfolobus / enzymology*

Substances

Bacterial Proteins
DNA-Directed DNA Polymerase