5FGH
Yeast 20S proteasome beta5-K33A mutant (propeptide expressed in trans) in complex with MG132
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 | 2015-12-10 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 136.920, 299.860, 145.980 |
| Unit cell angles | 90.00, 113.13, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.800 |
| R-factor | 0.18 |
| Rwork | 0.178 |
| R-free | 0.20600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ryp |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.855 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.079 | 0.486 |
| Number of reflections | 257992 | |
| <I/σ(I)> | 11.7 | 3 |
| Completeness [%] | 97.3 | 98 |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | 20 mM MgAC2, 13% MPD, 0.1 M MES |
