6UIY
Artificial Iron Proteins: Modelling the Active Sites in Non-Heme Dioxygenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-05-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 57.740, 57.740, 184.270 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 55.100 - 1.470 |
| R-factor | 0.154 |
| Rwork | 0.153 |
| R-free | 0.17680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qcb |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.434 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 55.100 | 55.100 | 1.490 |
| High resolution limit [Å] | 1.470 | 8.040 | 1.470 |
| Rmerge | 0.069 | 0.050 | 0.501 |
| Rmeas | 0.072 | 0.053 | 0.529 |
| Rpim | 0.020 | 0.017 | 0.170 |
| Total number of observations | 351473 | 2186 | 12637 |
| Number of reflections | 27259 | 215 | 1317 |
| <I/σ(I)> | 21.6 | 35.9 | 4 |
| Completeness [%] | 100.0 | 98.5 | 100 |
| Redundancy | 12.9 | 10.2 | 9.6 |
| CC(1/2) | 0.999 | 0.997 | 0.928 |
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 |
