1Q5R
The Rhodococcus 20S proteasome with unprocessed pro-peptides
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2000-10-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 152.094, 212.365, 250.213 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 3.100 |
| R-factor | 0.229 |
| Rwork | 0.229 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 23.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 3.100 |
| Rmerge | 0.084 |
| Number of reflections | 66375 |
| Completeness [%] | 88.7 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 * | 298 | 14% PEG 6000, 50mM sodium citrate, pH 5.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | pH7.0 |
| 3 | 1 | reservoir | PEG6000 | 14 (%(w/v)) | |
| 4 | 1 | reservoir | sodium citrate | 50 (mM) | pH5.4 |






