1B8X
GLUTATHIONE S-TRANSFERASE FUSED WITH THE NUCLEAR MATRIX TARGETING SIGNAL OF THE TRANSCRIPTION FACTOR AML-1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 85 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 93.400, 93.400, 57.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.700 |
| R-factor | 0.209 * |
| Rwork | 0.209 |
| R-free | 0.31000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gne |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.820 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.110 * | 0.250 * |
| Number of reflections | 7449 | |
| <I/σ(I)> | 3 | 2.5 |
| Completeness [%] | 94.9 | 87.5 |
| Redundancy | 2.5 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEG 4000 | ||
| 2 | 1 | 1 | PEG 400 | ||
| 3 | 1 | 1 | NA2HPO4 | ||
| 4 | 1 | 1 | NAH2PO4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 40 (%) | |
| 3 | 1 | reservoir | PEG400 | 2 (%) | |
| 4 | 1 | reservoir | 0.2 (M) |
