3VON
Crystalstructure of the ubiquitin protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-05-20 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 102.064, 137.285, 257.109 |
| Unit cell angles | 90.00, 90.03, 90.00 |
Refinement procedure
| Resolution | 50.000 - 3.150 |
| R-factor | 0.22601 |
| Rwork | 0.223 |
| R-free | 0.28060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 2ZFY and 1J7D |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.009 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.200 |
| High resolution limit [Å] | 3.150 | 3.150 |
| Rmerge | 0.083 | 0.322 |
| Number of reflections | 121981 | |
| <I/σ(I)> | 16.1 | 3.08 |
| Completeness [%] | 96.9 | 92.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 90mM Tris-HCl buffer (pH 8.5), 19% PEG 3350, 10mM EDTA sodium salt, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
