3HVP
CONSERVED FOLDING IN RETROVIRAL PROTEASES. CRYSTAL STRUCTURE OF A SYNTHETIC HIV-1 PROTEASE
Experimental procedure
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 50.240, 50.240, 106.560 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | ? - 2.800 |
| R-factor | 0.184 |
| RMSD bond length | 0.026 |
| RMSD bond angle | 0.076 |
| Refinement software | PROFFT |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.800 * |
| Rmerge | 1.500 * |
| Number of reflections | 3225 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG14000 | 12.5 (%(w/v)) | |
| 2 | 1 | reservoir | ammonium sulfate | 10-30 (%) | |
| 3 | 1 | drop | protein | 1mg |






