5KUT
hMiro2 C-terminal GTPase domain, GDP-bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-26 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.978720 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 80.610, 122.760, 103.890 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.576 - 1.693 |
| R-factor | 0.219 |
| Rwork | 0.218 |
| R-free | 0.23850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4c0l |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.640 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.800 | |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.085 | |
| Number of reflections | 57061 | |
| <I/σ(I)> | 10.1 | |
| Completeness [%] | 99.2 | |
| Redundancy | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 14 mg/mL protein, 0.2 M magnesium formate, 20% w/v PEG3350 |






