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 |