1HHP
THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE HIV-1 ISOLATE BRU
Experimental procedure
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 50.200, 50.200, 106.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 * - 2.700 |
| R-factor | 0.19 * |
| Rwork | 0.190 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 3.800 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 6.000 * |
| High resolution limit [Å] | 2.700 * |
| Rmerge | 0.098 * |
| Total number of observations | 3901 * |
| Number of reflections | 3549 * |
| Completeness [%] | 93.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | 4 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | HIV-protase | 1.1 (mg/ml) | |
| 2 | 1 | reservior | MOPS | 100 (mM) | |
| 3 | 1 | reservoir | 10 (%(w/v)) | ||
| 4 | 1 | reservoir | 0.4 (%(w/v)) |






