3WYO
Heterodimeric myoglobin formed by domain swapping
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-07-11 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.702, 72.168, 161.520 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.22795 |
| Rwork | 0.226 |
| R-free | 0.26616 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wla |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.507 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.073 | 0.630 |
| Number of reflections | 45097 | |
| <I/σ(I)> | 27 | 2.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.5 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 25% (w/v) PEG 1000, 100mM MES-NaOH buffer, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
