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  • Title: Crystallization and preliminary X-ray crystallographic analysis of DNA polymerase from Thermus aquaticus.
    Author: Eom SH, Song HK, Suh SW, Kim Y, Steitz TA, Park JH, Kim JS, Kwon ST, Lee DS.
    Journal: Acta Crystallogr D Biol Crystallogr; 1995 Nov 01; 51(Pt 6):1086-8. PubMed ID: 15299782.
    Abstract:
    Two crystal forms of DNA polymerase from Thermus aquaticus have been grown at room temperature. Rhombohedral crystals (form I) grown from ammonium sulfate solution diffracted poorly to 10 A only and thus are not suitable for X-ray structure determination. Trigonal crystals (form II) grown from polyethylene glycol solution are more suitable for structure determination since their diffraction pattern extends to 2.5 A at cryogenic temperature upon exposure to synchrotron X-rays. They belong to space group P3(1)21 (or its enantiomorph P3(2)21) and their unit-cell dimensions are a = 106.7 and c = 169.7 A, for flash-frozen crystals. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (V(M)) of 3.0 A(3) Da(-l) and a solvent content of 58% by volume. X-ray data have been collected to 2.7 A Bragg spacing from native crystals.
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