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      HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization

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          Abstract

          High-resolution X-ray crystallographic structures of HIV-1 protease clinical variants complexed with licensed inhibitors are essential to understanding the fundamental cause of protease drug resistance. There is a need for structures of naturally evolved HIV-1 proteases from patients failing antiretroviral therapy. Here, we report the expression, purification, and crystallization of clinical isolates of HIV-1 protease that have been characterized to be more than 100 times less susceptible to US FDA approved protease inhibitors.

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          Author and article information

          Journal
          Protein Expression and Purification
          Protein Expression and Purification
          Elsevier BV
          10465928
          March 2003
          March 2003
          : 28
          : 1
          : 165-172
          Article
          10.1016/S1046-5928(02)00650-2
          12651121
          b1240e55-666e-412f-bf4d-7444dc3b09e4
          © 2003

          https://www.elsevier.com/tdm/userlicense/1.0/

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