6UI0
Artificial Iron Proteins: Modelling the Active Sites in Non-Heme Dioxygenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-06-05 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 57.889, 57.889, 184.653 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.450 - 1.400 |
| R-factor | 0.1628 |
| Rwork | 0.162 |
| R-free | 0.17950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qcb |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.072 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.450 | 37.420 | 1.420 |
| High resolution limit [Å] | 1.400 | 7.670 | 1.400 |
| Rmerge | 0.065 | 0.035 | 2.333 |
| Rmeas | 0.066 | 0.035 | 2.379 |
| Rpim | 0.013 | 0.007 | 0.461 |
| Total number of observations | 5624 | 40363 | |
| Number of reflections | 31551 | 248 | 1533 |
| <I/σ(I)> | 30.6 | 113.3 | 1.7 |
| Completeness [%] | 100.0 | 99.2 | 100 |
| Redundancy | 25.9 | 22.7 | 26.3 |
| CC(1/2) | 1.000 | 1.000 | 0.679 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 295 | 26 mg/mL protein, 2.0 Ammonium Sulfate, 0.1 M sodium acetate pH 4 |
