5K16
Crystal structure of free Ubiquitin-specific protease 12
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-05-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.396, 109.636, 134.193 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.451 - 2.599 |
R-factor | 0.1927 |
Rwork | 0.190 |
R-free | 0.24590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3m99 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.232 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (dev_1760) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.599 | 2.599 |
Rmerge | 0.091 | 0.740 |
Number of reflections | 24515 | |
<I/σ(I)> | 14.3 | 1.4 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 0.1 M Tris-HCl, 18% PEG 3350, 0.2 M Lithium Sulfate |