1HMV
THE STRUCTURE OF UNLIGANDED REVERSE TRANSCRIPTASE FROM THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
Experimental procedure
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 168.700, 162.800, 331.800 |
| Unit cell angles | 90.00, 105.70, 90.00 |
Refinement procedure
| Resolution | 6.000 - 3.200 |
| R-factor | 0.254 |
| Rwork | 0.254 |
| R-free | 0.29700 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.245 * |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 3.200 * |
| Rmerge | 0.133 * |
| Number of reflections | 120337 |
| Completeness [%] | 85.0 |
| Redundancy | 3.3 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.8 * | 4 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 30 (mg/ml) | |
| 2 | 1 | drop | sodium phosphate | 75 (mM) | |
| 3 | 1 | drop | dithiothreitol | 1-2 (mM) | |
| 4 | 1 | reservoir | ammonium sulfate | 33-35 (%) | |
| 5 | 1 | reservoir | sodium phospahte | 100 (mM) |
