Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon.

Autor: Zhou M; Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA., Mao C, Rodriguez AC, Kiefer JR, Kucera RB, Beese LS
Jazyk: angličtina
Zdroj: Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 1998 Sep 01; Vol. 54 (Pt 5), pp. 994-5.
DOI: 10.1107/s0907444998001553
Abstrakt: The hyperthermostable DNA polymerase from a marine Thermococcus archaeon has been crystallized in space group P212121, with unit-cell dimensions a = 94.8, b = 98.2, c = 112.2 A with one molecule per asymmetric unit. Conditions for data collection at 98 K have been identified, and a complete data set was collected to 2.2 A resolution. Strategies employed here may facilitate crystallization of other hyperthermostable proteins. The structure of this enzyme will provide the first structural data on the archaeal and hyperthermostable classes of DNA polymerases. Sequence homology to human polymerase alpha (polymerase B family) may make it a model for studying eukaryotic and viral polymerases and for the development of anti-cancer and anti-viral therapeutics.
Databáze: MEDLINE