2HTH
Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-02-12 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.10000, 0.97910 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 102.727, 102.727, 54.306 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.320 - 2.700 |
R-factor | 0.25184 |
Rwork | 0.248 |
R-free | 0.28872 |
Structure solution method | SAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.681 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE (2.10) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.800 |
High resolution limit [Å] | 2.700 | 5.810 | 2.700 |
Rmerge | 0.109 | 0.080 | 0.536 |
Number of reflections | 8264 | ||
<I/σ(I)> | 11 | ||
Completeness [%] | 97.7 | 99.6 | 81.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 10% PEG8000; 10% Ethylene glycol; 100mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |