Abstract
Two crystal forms of complexes have been grown that contain human immunodeficiency virus type 1 reverse transcriptase and a monoclonal antibody Fab fragment. One of the crystal forms (form II, space group P3112, a = 168.7 A, c = 220.3 A) diffracts x-rays to 3.5-A resolution and appears suitable for moderate-resolution structure determination. The form II crystals have the unusual property that their maximum resolution of diffraction and resistance to radiation damage are enhanced by either crystallization in the presence of or soaking with double-stranded DNA primer-template mimics. These crystals may permit structural studies of catalytically relevant complexes and eventually enable us to experimentally observe successive steps in the reverse transcription process.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Antibodies, Monoclonal* / isolation & purification
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Base Sequence
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Escherichia coli / genetics
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HIV-1 / enzymology*
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Immunoglobulin Fab Fragments* / isolation & purification
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Molecular Sequence Data
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Oligodeoxyribonucleotides / chemistry*
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Oligodeoxyribonucleotides / metabolism
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Protein Binding
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RNA-Directed DNA Polymerase / chemistry*
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RNA-Directed DNA Polymerase / immunology
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RNA-Directed DNA Polymerase / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / immunology
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Recombinant Proteins / metabolism
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X-Ray Diffraction / methods
Substances
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Antibodies, Monoclonal
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Immunoglobulin Fab Fragments
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Oligodeoxyribonucleotides
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Recombinant Proteins
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RNA-Directed DNA Polymerase