8OEM
Crystal structure of FutA bound to Fe(II)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 294 |
| Detector technology | PIXEL |
| Collection date | 2018-01-16 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.361, 78.011, 47.994 |
| Unit cell angles | 90.00, 98.23, 90.00 |
Refinement procedure
| Resolution | 47.500 - 1.700 |
| Rwork | 0.153 |
| R-free | 0.18040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.879 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.500 | 47.500 | 1.730 |
| High resolution limit [Å] | 1.700 | 9.000 | 1.700 |
| Rmerge | 0.053 | 0.026 | 0.403 |
| Rmeas | 0.054 | 0.026 | 0.412 |
| Rpim | 0.009 | 0.005 | 0.085 |
| Number of reflections | 30881 | 232 | 1369 |
| <I/σ(I)> | 71.7 | 175.1 | 11.6 |
| Completeness [%] | 97.9 | 99.8 | 83.5 |
| Redundancy | 65.4 | 56.7 | 42.1 |
| CC(1/2) | 1.000 | 1.000 | 0.986 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 294 | Purified protein and crystallisation buffer were mixed at a 1:1 ratio. Crystallisation buffer was 20% PEG 3350, 200 mM sodium thiocyanate. |
