The growth and characterization of crystals of human immunodeficiency virus (HIV) reverse transcriptase
Jones EY., Stuart DI., Garman EF., Griest R., Phillips DC., Taylor GL., Matsumoto O., Darby G., Larder B., Lowe D., Powell K., Purifoy D., Ross CK., Somers D., Tisdale M., Stammers DK.
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 Å or better. Type 1 crystals belong to the space group P212121 with unit cell dimensions a = 147 A ̊, b = 190 A ̊ and c = 182 A ̊. Crystal density measurement 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 P4222 with unit cell dimensions a = b = 120 A ̊, c = 320 A ̊) 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 (7%; 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. © 1993.