8OEI
SFX structure of FutA after an accumulated dose of 350 kGy
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | FREE ELECTRON LASER |
| Source details | SACLA BEAMLINE BL2 |
| Synchrotron site | SACLA |
| Beamline | BL2 |
| Temperature [K] | 298 |
| Detector technology | CCD |
| Collection date | 2022-05-10 |
| Detector | MPCCD |
| Wavelength(s) | 1.126 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.366, 78.220, 48.025 |
| Unit cell angles | 90.00, 97.90, 90.00 |
Refinement procedure
| Resolution | 32.441 - 1.650 |
| Rwork | 0.160 |
| R-free | 0.18850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.572 |
| Data reduction software | DIALS |
| Data scaling software | cctbx.xfel.merge |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.441 | 1.679 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rpim | 0.691 | |
| Number of reflections | 34653 | 1676 |
| <I/σ(I)> | 3.7 | 0.43 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 165.2 | 82.4 |
| CC(1/2) | 0.970 | 0.400 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 294 | Purified protein, diluted crystal seeds, and crystallisation buffer were mixed at a 1:1.5:1.5 ratio. Crystallisation buffer was 25% PEG 3350, 200 mM sodium thiocyanate. Crystal seed stock was diluted 1:20 in 25% PEG 3350. |
