9AVD
Mitochondrial fission 1 protein Fis1 structure T34D mutation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-05-10 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 43.510, 43.510, 120.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.300 - 2.510 |
| R-factor | 0.2373 |
| Rwork | 0.234 |
| R-free | 0.28780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.091 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.300 | 35.300 | 2.580 |
| High resolution limit [Å] | 2.510 | 11.230 | 2.510 |
| Rmerge | 0.094 | 0.053 | 1.816 |
| Rmeas | 0.098 | 0.056 | 1.873 |
| Number of reflections | 4385 | 66 | 327 |
| <I/σ(I)> | 14.29 | ||
| Completeness [%] | 100.0 | ||
| Redundancy | 16.2 | ||
| CC(1/2) | 0.998 | 0.998 | 0.825 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 292 | 0.2M Sodium Bromide, 20% PEG 3350 |






