Purification and characterization of an active human immunodeficiency virus type 1 RNase H domain.

@article{Smith1993PurificationAC,
  title={Purification and characterization of an active human immunodeficiency virus type 1 RNase H domain.},
  author={Jean S. Smith and Monica J Roth},
  journal={Journal of virology},
  year={1993},
  volume={67 7},
  pages={
          4037-49
        }
}
We have expressed and purified from Escherichia coli a human immunodeficiency virus type 1 (HIV-1) RNase H domain consisting of amino acids 400 to 560 of reverse transcriptase with either an N- or C-terminal polyhistidine tag. The native protease cleavage site of HIV-1 reverse transcriptase is between amino acids 440 and 441. Purification on Ni(2+)-nitrilotriacetate agarose resulted in a highly active RNase H domain dependent on MnCl2 rather than MgCl2. Activity was unambiguously attributed to… CONTINUE READING

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