2I6T
Orthorhombic Structure of the LDH domain of Human Ubiquitin-conjugating Enzyme E2-like Isoform A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-07-19 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 53.088, 98.912, 126.753 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.550 - 2.100 |
| R-factor | 0.18267 |
| Rwork | 0.180 |
| R-free | 0.23004 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1i10 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.412 |
| 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] | 26.550 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 39716 | |
| <I/σ(I)> | 12.6 | 2.88 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 26% PEG3350, 0.2 M ammonium sulfate, 0.1 M sodium cacodylate, pH 5.2 in protein buffer comprising of 20 mM Tris-HCl, pH 8.0, 500 mM NaCl, 5% glycerol, 10 mM dithiothreitol, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |






