3E46
Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting protein 2) M172A mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-07 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97000 |
Spacegroup name | I 4 |
Unit cell lengths | 134.490, 134.490, 38.404 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.380 - 1.860 |
R-factor | 0.174 |
Rwork | 0.172 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bep |
RMSD bond length | 0.018 |
RMSD bond angle | 1.514 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.910 |
High resolution limit [Å] | 1.860 | 1.860 |
Number of reflections | 27414 | |
<I/σ(I)> | 1.98 | |
Completeness [%] | 93.4 | 52.4 |
Redundancy | 4 | 1.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | Calcium acetate, Sodium acetate, NaCl, PEG 8000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |