2C7M
Human Rabex-5 residues 1-74 in complex with Ubiquitin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-09-03 |
| Detector | ADSC CCD |
| Spacegroup name | P 61 |
| Unit cell lengths | 81.900, 81.900, 55.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.670 - 2.400 |
| R-factor | 0.184 |
| Rwork | 0.183 |
| R-free | 0.21400 |
| Structure solution method | SAD |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.380 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | HKL2Map |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.040 | 0.220 |
| Number of reflections | 8066 | |
| <I/σ(I)> | 43.11 | 6 |
| Completeness [%] | 96.1 | 76.9 |
| Redundancy | 18.5 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | SITTING DROP 300 NL PLUS 300 NL 20 MG/ML PROTEIN SOLUTION 0.2 M LIS2SO4, 0.1 MES PH 6.5 25% PEG3350 |
