5IZA
Protein-protein interaction
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 93 |
Detector technology | PIXEL |
Collection date | 2015-06-15 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.978 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.465, 66.436, 82.661 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 51.780 - 1.500 |
R-factor | 0.12252 |
Rwork | 0.121 |
R-free | 0.15921 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nmw |
RMSD bond length | 0.011 |
RMSD bond angle | 1.452 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.780 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.545 | 0.545 |
Number of reflections | 46357 | |
<I/σ(I)> | 21.27 | 2.86 |
Completeness [%] | 99.5 | 99.9 |
Redundancy | 4.7 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 0.2M Ammonium sulfate, 0.1M Tris pH 8.0, 25% w/v PEG 4000 |