21LS
Crystal structure of Horse spleen L-ferritin mutant (L24G/S27G/E56A/R59G/E60A/E63A)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E DW |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2023-11-13 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | F 4 3 2 |
| Unit cell lengths | 181.566, 181.566, 181.566 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.700 - 1.570 |
| R-factor | 0.2038 |
| Rwork | 0.203 |
| R-free | 0.22190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.849 |
| Data reduction software | CrysalisPro |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.700 | 1.600 |
| High resolution limit [Å] | 1.570 | 1.570 |
| Rmerge | 0.060 | 0.897 |
| Rmeas | 0.063 | 0.965 |
| Rpim | 0.018 | 0.352 |
| Number of reflections | 36283 | 1766 |
| <I/σ(I)> | 25.7 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.7 | 7.4 |
| CC(1/2) | 1.000 | 0.862 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | Ammonium sulfate, Cadmium sulfate |






