2AWF
Structure of human Ubiquitin-conjugating enzyme E2 G1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-23 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.97985 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 59.444, 59.444, 186.812 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.980 - 2.100 |
| R-factor | 0.22289 |
| Rwork | 0.221 |
| R-free | 0.26337 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pzv |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.570 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.700 | 2.080 |
| High resolution limit [Å] | 2.010 | 2.010 |
| Rmerge | 0.037 | 0.647 |
| Number of reflections | 13412 | |
| <I/σ(I)> | 72.07 | 2.25 |
| Completeness [%] | 96.4 | 84.6 |
| Redundancy | 15.5 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 24% PEG3350, 0.2 M MgAc, 0.1 M Tris, pH 7.5, 5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
