The growth and characterization of crystals of human-immunodeficiency-virus (hiv) reverse-transcriptase

E Y JONES, D I STUART, E F GARMAN, R GRIEST, D C PHILLIPS, G L TAYLOR, O MATSUMOTO, G DARBY, B LARDER, D LOWE, K POWELL, D PURIFOY, C K ROSS, D SOMERS, M TISDALE, D K STAMMERS

Research output: Contribution to journalArticlepeer-review

Abstract

Extensive studies on the crystallization of HIV-1 reverse transcriptase (RT) have yielded several crystal forms, two of which show diffraction to minimum Bragg spacings of 6 angstrom or better. Type 1 crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions a = 147 angstrom, b = 190 angstrom and c = 182 angstrom. Crystal density measurements indicate a very high crystal solvent content of 77% consistent with the presence of two RT heterodimers (66k/51k) per crystallographic asymmetric unit. These crystals are suitable for a low resolution determination of the apoenzyme structure. The second well ordered crystal form (space group P4(2)22 with unit cell dimensions a = b = 120 angstrom, c = 320 angstrom) results from the co-crystallization of RT heterodimer and a double-stranded DNA oligonucleotide. Crystal density measurements again yield a relatively high value for the solvent content (70%; one RT heterodimer per crystallographic asymmetric unit) and elemental analysis indicates that one DNA oligonucleotide is associated with each RT heterodimer. This is consistent with each heterodimer possessing a single, competent, active site.

Original languageEnglish
Pages (from-to)261-269
Number of pages9
JournalJournal of Crystal Growth
Volume126
Issue number2-3
Publication statusPublished - Jan 1993

Keywords

  • MACROMOLECULAR CRYSTALLOGRAPHY
  • WEISSENBERG CAMERA
  • H DOMAIN
  • CRYSTALLIZATION
  • PURIFICATION
  • EXPRESSION
  • RESOLUTION

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