Expression, Purification, and Crystallization of the HIV-1 Reverse Transcriptase (RT)
- 1 November 1990
- journal article
- research article
- Published by Mary Ann Liebert Inc in AIDS Research and Human Retroviruses
- Vol. 6 (11) , 1297-1303
- https://doi.org/10.1089/aid.1990.6.1297
Abstract
The HIV-1 pol gene proteins (protease, reverse transcriptase, and endonuclease) were expressed in Escherichia coli N4830-1 by the use of the inducible expression vector pWS60 into which the pol gene was inserted. The p66/p51 heterodimer of reverse transcriptase (RT) was isolated in a highly pure and active form. Crystals of the p66/p51 heterodimer were obtained by the vapor diffusion hanging drop technique. The present crystal quality is still not adequate for high resolution X-ray investigation.This publication has 31 references indexed in Scilit:
- Point mutations in conserved amino acid residues within the C‐terminal domain of HIV‐1 reverse transcriptase specifically repress RNase H functionFEBS Letters, 1989
- HIV-1 reverse transcriptase: crystallization and analysis of domain structure by limited proteolysisBiochemistry, 1988
- Structural Requirements for Bacterial Expression of Stable, Enzymatically Active Fusion Proteins Containing the Human Immunodeficiency Virus Reverse TranscriptaseDNA, 1988
- Site-specific mutagenesis of AIDS virus reverse transcriptaseNature, 1987
- Applying knowledge of protein structure and functionTrends in Biotechnology, 1987
- Protein Crystallography and Computer Graphics—toward Rational Drug DesignAngewandte Chemie International Edition in English, 1986
- Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAVScience, 1986
- Monoclonal Antibodies to Herpes Simplex Virus Thymidine KinaseJournal of General Virology, 1984
- Drug design by the method of receptor fitJournal of Medicinal Chemistry, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970