5IA8
Structure of a Ubiquitin like protein with an E1 fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.918409 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 46.940, 46.940, 201.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.300 - 2.000 |
| R-factor | 0.22212 |
| Rwork | 0.221 |
| R-free | 0.23627 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5iaa |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.449 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.300 | |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.096 | |
| Number of reflections | 16255 | |
| Completeness [%] | 100.0 | |
| Redundancy | 10.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 0.2M Potassium phosphate dibasic and 20% PEG 3350 |
