3QIP
Structure of HIV-1 reverse transcriptase in complex with an RNase H inhibitor and nevirapine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-02-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 118.898, 154.876, 153.079 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.354 - 2.093 |
| R-factor | 0.2188 |
| Rwork | 0.216 |
| R-free | 0.26690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vrt |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.091 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.140 |
| High resolution limit [Å] | 2.093 | 2.093 |
| Rmerge | 0.046 | 0.500 |
| Number of reflections | 82059 | |
| <I/σ(I)> | 29.3 | 2.1 |
| Completeness [%] | 98.9 | 87.9 |
| Redundancy | 5.6 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 1.3M (NH4)2SO4, 5mM sodium malonate, and 100mM cacodylate pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
