9WX5
Crystal structure of frog M-ferritin E130A_M161E mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 2015-05-13 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9794 |
| Spacegroup name | F 4 3 2 |
| Unit cell lengths | 184.032, 184.032, 184.032 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.190 - 1.500 |
| Rwork | 0.128 |
| R-free | 0.16300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ka3 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.984 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0431 (REFMACAT 0.4.105)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.190 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Number of reflections | 43133 | 3127 |
| <I/σ(I)> | 27.3 | |
| Completeness [%] | 100.0 | |
| Redundancy | 14.2 | |
| CC(1/2) | 1.000 | 0.963 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277.15 | 2.0 M MgCl2 and 100 mM Bicine (pH 9.0) |






