1YLA
Ubiquitin-conjugating enzyme E2-25 kDa (Huntington interacting protein 2)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-12-10 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 1 |
Unit cell lengths | 37.831, 55.022, 61.762 |
Unit cell angles | 64.19, 74.61, 69.89 |
Refinement procedure
Resolution | 30.000 - 2.400 |
R-factor | 0.225 |
Rwork | 0.225 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tte |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.054 | 0.164 |
Number of reflections | 15647 | |
<I/σ(I)> | 11 | 3 |
Completeness [%] | 96.1 | 96.1 |
Redundancy | 2.23 | 2.21 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | PEG 8000, calcium acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K, pH 6.50 |