1UCH
DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.600, 60.900, 81.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.800 |
| R-factor | 0.232 |
| Rwork | 0.232 |
| R-free | 0.29400 |
| Structure solution method | MAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 25.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.843) |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.040 | 0.190 |
| Number of reflections | 23334 | |
| <I/σ(I)> | 20 | 5 |
| Completeness [%] | 98.0 | 93 |
| Redundancy | 4.5 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.7 | 4 * | PROTEIN AT 12 MG/ML WAS CRYSTALLIZED FROM 26%(W/W) PEG 4000, 200 MM SODIUM ACETATE, 100 MM PIPES PH 6.7 AND 10 MM DTT IN SITTING WELLS AT 4 DEGREES CELSIUS., vapor diffusion - sitting drop, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | beta-mercaptoethanol | 15 (mM) | |
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | reservoir | PEG4000 | 26 (%(w/v)) | |
| 6 | 1 | reservoir | sodium acetate | 200 (mM) | |
| 7 | 1 | reservoir | PIPES | 100 (mM) | |
| 8 | 1 | reservoir | dithiothreitol | 10 (mM) |
