9VIW
Structure of Thermocrinis minervae double ferritin-like protein (ThmDFLP)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17UM |
| Synchrotron site | SSRF |
| Beamline | BL17UM |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-05-25 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.955, 105.160, 89.144 |
| Unit cell angles | 90.00, 90.27, 90.00 |
Refinement procedure
| Resolution | 46.546 - 2.466 |
| Rwork | 0.243 |
| R-free | 0.29310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AF-A0A1M6SI41-F1 |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.546 |
| Data reduction software | XDS |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.503 | 2.716 |
| High resolution limit [Å] | 2.453 | 2.453 |
| Rmerge | 0.345 | 1.595 |
| Rmeas | 0.374 | 1.720 |
| Rpim | 0.142 | 0.638 |
| Number of reflections | 28140 | 1407 |
| <I/σ(I)> | 5.1 | 1.4 |
| Completeness [%] | 65.1 | |
| Completeness (spherical) [%] | 12.5 | |
| Completeness (ellipsoidal) [%] | 59.9 | |
| Redundancy | 6.9 | 7.2 |
| CC(1/2) | 0.982 | 0.598 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 293 | 40% v/v Ethanol, 5% w/v PEG 1000, 0.1 M Phosphate/citrate buffer, pH 4.2 |
