5WBB
Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - S112A
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 | 2016-12-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 57.640, 57.640, 183.980 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 55.000 - 1.500 |
| R-factor | 0.15779 |
| Rwork | 0.156 |
| R-free | 0.18803 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qcb |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.785 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Number of reflections | 25455 | |
| <I/σ(I)> | 13.3 | |
| Completeness [%] | 100.0 | |
| Redundancy | 9.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 298 | 0.1 M sodium acetate, 2.6 M sodium sulfate |
