3UNF
Mouse 20S immunoproteasome in complex with PR-957
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06DA |
Synchrotron site | SLS |
Beamline | X06DA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-12 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 117.300, 194.600, 157.700 |
Unit cell angles | 90.00, 107.10, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.900 |
R-factor | 0.23724 |
Rwork | 0.235 |
R-free | 0.27498 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1iru |
RMSD bond length | 0.005 |
RMSD bond angle | 0.926 |
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 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.116 | 0.547 |
Number of reflections | 145087 | |
<I/σ(I)> | 8 | 2 |
Completeness [%] | 97.1 | 89.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 | 0.2 M NaI, 40% MPD, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |