8BHX
High resolution structure of the iron Superoxide Dismutase from Thermobifida fusca
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-08-18 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.918400 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 98.610, 58.590, 67.940 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.650 - 1.250 |
| R-factor | 0.1258 |
| Rwork | 0.125 |
| R-free | 0.14450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bsm |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.133 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.700 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.033 | 0.347 |
| Number of reflections | 108003 | 9675 |
| <I/σ(I)> | 10.05 | 1.86 |
| Completeness [%] | 98.8 | 89.74 |
| Redundancy | 5.3 | |
| CC(1/2) | 0.998 | 0.673 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | 25% (w/v) PEG 1500 and 0.1 M sodium malonate dibasic monohydrate, imidazole and boric acid buffer at pH 8.0, from a PACT premier screen |
