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 (%) |