1BIZ
HIV-1 INTEGRASE CORE DOMAIN
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 95 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-11 |
| Detector | RIGAKU |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.840, 71.340, 91.880 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | ? - 1.950 |
| R-factor | 0.212 |
| Rwork | 0.212 |
| R-free | 0.25300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1itg |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.490 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.100 | |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.054 | 0.237 |
| Number of reflections | 20883 | |
| Completeness [%] | 92.3 | 88.4 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 * | PROTEIN WAS CRYSTALLIZED FROM 30% PEG 4000, 100 MM HEPES, PH 7.0, 5 MM DTT |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 0.5 (M) | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | dithiothreitol | 5 (mM) | |
| 6 | 1 | reservoir | PEG8000 | 15 (%) | |
| 7 | 1 | reservoir | ammonium sulfate | 0.16 (M) | |
| 8 | 1 | reservoir | sodium cacodylate | 100 (mM) | |
| 9 | 1 | reservoir | dithiothreitol | 5 (mM) |
