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 |