2A4D
Structure of the human ubiquitin-conjugating enzyme E2 variant 1 (UEV-1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-06-08 |
| Detector | RIGAKU RAXIS IV++ |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 43.058, 53.910, 108.034 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.690 |
| R-factor | 0.185 |
| Rwork | 0.183 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1j7d |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.552 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.750 |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.038 | 0.332 |
| Number of reflections | 13994 | |
| <I/σ(I)> | 44 | 2.7 |
| Completeness [%] | 96.4 | 96.4 |
| Redundancy | 5.9 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 298 | 32% PEG1500, 0.2 M NaCl, 1 mM DTT, 0.1 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 6.50 |
