1MH3
maltose binding-a1 homeodomain protein chimera, crystal form I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 95.485, 95.485, 155.887 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 60.000 * - 2.100 |
Rwork | 0.232 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MBP (pdb code 4MBP) |
RMSD bond length | 0.006 |
RMSD bond angle | 1.160 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 * | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.057 * | 0.216 * |
Number of reflections | 42612 | |
<I/σ(I)> | 30.1 | 4.9 |
Completeness [%] | 99.2 | 97.1 |
Redundancy | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | amonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | MES | 100 (mM) | pH5.0 |
3 | 1 | reservoir | ammonium sulfate | 2.4 (M) |