2OB4
Human Ubiquitin-Conjugating Enzyme CDC34
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 | 2005-12-18 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97917 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 42.280, 66.310, 124.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.030 - 2.400 |
R-factor | 0.22637 |
Rwork | 0.223 |
R-free | 0.28448 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.410 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.450 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 7162 | |
<I/σ(I)> | 2.64 | 2.6 |
Completeness [%] | 99.5 | 94.8 |
Redundancy | 1.82 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | The protein was dissolved at 42 mg/ml in 20 mM Tris-HCl, pH 8.0, 0.15 M NaCl, 5% glycerol and 2 mM DTT. Crystals were grown in hanging drops by mixing 2 microL protein solution with 2 microL well solution (28% PEG 4000, 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, 1 mM DTT and 7.5 mM glycyl-glycyl-glycine) at 21 deg C. For cryoprotection, the crystals were soaked in the well solution supplemented with 25% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 298K |