2NQ3
Crystal structure of the C2 Domain of Human Itchy Homolog E3 Ubiquitin Protein Ligase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-09-09 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 82.499, 82.499, 65.273 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.100 - 1.800 |
R-factor | 0.16352 |
Rwork | 0.162 |
R-free | 0.19544 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2fk9 |
RMSD bond length | 0.018 |
RMSD bond angle | 1.600 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 24173 | |
<I/σ(I)> | 29.2 | 3.4 |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.7 | 10.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | The protein at 20 mg/ml was dissolved in 20 mM Tris-HCl, pH 8.0, 0.15 M NaCl, 5% glycerol, 2 mM DTT, and mixed 1:1 with well solution that was 20% PEG3350, 0.1 M bis-Tris, pH 6.0, 0.2 M NH4OAc, 1 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |