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 |