3BZH
Crystal structure of human ubiquitin-conjugating enzyme E2 E1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-01-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97942 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 51.630, 51.630, 109.437 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.000 - 1.600 |
| R-factor | 0.20639 |
| Rwork | 0.205 |
| R-free | 0.22571 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1y6l |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.347 |
| 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] | 40.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Number of reflections | 22998 | |
| <I/σ(I)> | 64.3816 | 2.42 |
| Completeness [%] | 99.8 | 99.6 |
| Redundancy | 10.2 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 298 | 2.2M (NH4)2SO4, 0.1M Bis-Tris-Propane pH 9.0, 0.001M DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
