6D71
Crystal Structure of the Human Miro1 N-terminal GTPase bound to GTP
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 | 2015-02-24 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.979130 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.350, 78.270, 99.780 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.070 - 1.718 |
| R-factor | 0.183706560744 |
| Rwork | 0.182 |
| R-free | 0.21989 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.784 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 61.500 | 1.750 |
| High resolution limit [Å] | 1.718 | 1.720 |
| Rmerge | 0.136 | 1.532 |
| Rmeas | 0.152 | 1.715 |
| Rpim | 0.067 | 0.759 |
| Number of reflections | 35285 | 3438 |
| <I/σ(I)> | 8.1 | 0.9 |
| Completeness [%] | 99.9 | 98.3 |
| Redundancy | 4.9 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 298 | 10 mg/mL protein + reservoir (0.6 M MMT, pH 5.0, 22% PEG1500) |
