1MI0
Crystal Structure of the redesigned protein G variant NuG2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 47.330, 73.790, 39.180 |
| Unit cell angles | 90.00, 96.00, 90.00 |
Refinement procedure
| Resolution | 15.000 * - 1.850 |
| R-factor | 0.291 |
| Rwork | 0.260 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.020 |
| RMSD bond angle | 3.800 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.840 | 1.930 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.067 * | |
| Number of reflections | 10905 * | |
| Completeness [%] | 97.3 * | 83 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 298 | ammonium sulfate, tris-hcl, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
| 2 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
| 3 | 1 | reservoir | Tris | 0.1 (M) | pH8.0 |






