Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution.

Journal article

Reverse transcriptase (RT) from the human immunodeficiency virus type 1 has been crystallized in four closely related forms, the best of which diffract X-rays to 2.2 A resolution. The RT was crystallized as a complex with a non-nucleoside inhibitor, either nevirapine or a nevirapine analogue. Crystals grew from 6% PEG 3400 buffered at pH 5. These were of space group P2(1)2(1)2(1) with unit cell parameters a = 147 A, b = 112 A, c = 79 A (form A), with one RT heterodimer in the asymmetric unit. Changes in unit cell parameters and degree of crystalline order were observed on soaking pregrown crystals in various solutions, giving three further sets of unit cells. These were a = 143 A, b = 112, A, c = 79 A (form B), a = 141 A, b = 111 A, c = 73 A (form C), a = 143 A, b = 117 A, c = 66.5 A (form D). The last two forms diffract X-rays to 2.2 A resolution. Structure determinations of these latter crystal forms of RT should give a detailed atomic model for this therapeutically important drug target.

Authors: Stammers, D; Somers, DO; Ross, C; Kirby, I; Ray, P

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 242
• Issue: 4
• Pages: 586-588
• Publication date: 1994-09-01
• DOI: 10.1006/jmbi.1994.1604
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Reverse Transcriptase Inhibitors; HIV-1; Crystallography, X-Ray; Pyridines; RNA-Directed DNA Polymerase; HIV Reverse Transcriptase; Nevirapine