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Title
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Crystallization and preliminary diffraction analysis of a hyperthermostable DNA polymerase from a Thermococcus archaeon.
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Authors
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M.Zhou,
C.Mao,
A.C.Rodriguez,
J.R.Kiefer,
R.B.Kucera,
L.S.Beese.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
994-995.
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PubMed id
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Abstract
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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.
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