1GY5
D92N,D94N double point mutant of human Nuclear Transport Factor 2 (NTF2)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 100 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.040, 79.020, 42.140 |
| Unit cell angles | 90.00, 104.36, 90.00 |
Refinement procedure
| Resolution | 18.000 - 2.300 |
| R-factor | 0.222 * |
| Rwork | 0.222 |
| R-free | 0.26400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.300 * |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 18.100 | |
| High resolution limit [Å] | 2.300 | 2.300 * |
| Rmerge | 0.450 | 0.092 * |
| Total number of observations | 18416 * | |
| Number of reflections | 7519 | |
| Completeness [%] | 96.6 | 91.7 * |
| Redundancy | 2.3 | 2.2 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 | 18 * | pH 4.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 8 (%) | |
| 2 | 1 | reservoir | sodium acetate | 100 (mM) | pH4.5 |
| 3 | 1 | reservoir | 50 (mM) | ||
| 4 | 1 | drop | protein | 2.8 (mg/ml) |






