8Q5F
Crystal structure of miniSOG protein from Arabidopsis thaliana with covalent FMN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-02-23 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.96456 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 62.821, 130.314, 67.426 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.650 - 2.000 |
| R-factor | 0.19035 |
| Rwork | 0.188 |
| R-free | 0.22839 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.491 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.430 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.068 | 0.980 |
| Rmeas | 0.078 | 1.114 |
| Rpim | 0.036 | 0.514 |
| Total number of observations | 69790 | 5601 |
| Number of reflections | 17411 | 1375 |
| <I/σ(I)> | 11.9 | 1.6 |
| Completeness [%] | 91.8 | |
| Redundancy | 4 | 4.1 |
| CC(1/2) | 0.999 | 0.697 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 19% polyacrylic acid 5100, 100 mM Hepes ppH 7.5 |
