6ANX
Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - WT (low exposure)
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 | 2017-08-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 57.640, 57.640, 183.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 54.990 - 1.620 |
R-factor | 0.16439 |
Rwork | 0.163 |
R-free | 0.18691 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2qcb |
RMSD bond length | 0.023 |
RMSD bond angle | 2.344 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 54.990 | 1.640 |
High resolution limit [Å] | 1.620 | 1.620 |
Number of reflections | 20471 | 995 |
<I/σ(I)> | 12.9 | 1.1 |
Completeness [%] | 100.0 | 99.5 |
Redundancy | 13.4 | 10.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4 | 274 | 2.6 M ammonium sulfate, 0.1 M sodium acetate |