1AXA
ACTIVE-SITE MOBILITY IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 PROTEASE AS DEMONSTRATED BY CRYSTAL STRUCTURE OF A28S MUTANT
Experimental procedure
| Temperature [K] | 293 |
| Detector technology | AREA DETECTOR |
| Collection date | 1996-05 |
| Detector | SIEMENS |
| Spacegroup name | P 61 |
| Unit cell lengths | 63.554, 63.554, 83.660 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| Rwork | 0.194 |
| Structure solution method | DIFFERENCE FOURIER |
| RMSD bond length | 0.019 |
| RMSD bond angle | 28.500 * |
| Data reduction software | SAINT |
| Data scaling software | SAINT |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.000 | 2.200 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.064 * | |
| Number of reflections | 11025 | |
| <I/σ(I)> | 15 | 3 |
| Completeness [%] | 93.0 | 75.9 * |
| Redundancy | 4.9 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.5 * | 20 * | pH 6.8 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protease | 4 (mg/ml) | |
| 2 | 1 | drop | sodium acetate | 10 (mM) | |
| 3 | 1 | drop | dithiothreitol | 0.5 (mM) | |
| 4 | 1 | drop | U89360E | 5 (M) | |
| 5 | 1 | drop | ammonium sulfate | 15 (%) | |
| 6 | 1 | reservoir | ammonium sulfate | 30 (%) |
