6UIU
Artificial Iron Proteins: Modelling the Active Sites in Non-Heme Dioxygenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-05-19 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 57.871, 57.871, 184.305 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.430 - 1.350 |
| R-factor | 0.208 |
| Rwork | 0.207 |
| R-free | 0.23020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qcb |
| RMSD bond length | 0.015 |
| RMSD bond angle | 3.027 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.3) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.430 | 37.400 | 1.370 |
| High resolution limit [Å] | 1.350 | 7.380 | 1.350 |
| Rmerge | 0.237 | 0.165 | 2.462 |
| Rmeas | 0.247 | 0.172 | 2.584 |
| Rpim | 0.067 | 0.046 | 0.757 |
| Total number of observations | 3455 | 18995 | |
| Number of reflections | 35163 | 275 | 1647 |
| <I/σ(I)> | 5.6 | 11.7 | 1.1 |
| Completeness [%] | 99.8 | 99.3 | 96.4 |
| Redundancy | 13.1 | 12.6 | 11.5 |
| CC(1/2) | 0.992 | 0.988 | 0.910 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 295 | 26 mg/mL protein, 2.0 M ammonium sulfate, 0.1 M sodium acetate pH 4 |
