3UNE
Mouse constitutive 20S proteasome
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-05-23 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 170.970, 201.300, 226.010 |
Unit cell angles | 90.00, 108.07, 90.00 |
Refinement procedure
Resolution | 15.000 - 3.200 |
R-factor | 0.22174 |
Rwork | 0.220 |
R-free | 0.24636 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1iru |
RMSD bond length | 0.004 |
RMSD bond angle | 0.753 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0119) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.300 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.076 | 0.597 |
Number of reflections | 235050 | |
<I/σ(I)> | 13.9 | 2.4 |
Completeness [%] | 99.5 | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 293 | 0.2 M KAc, 40% MPD, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K |