1W3B
The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Collection date | 2003-11-07 |
Spacegroup name | P 1 |
Unit cell lengths | 64.320, 75.510, 77.670 |
Unit cell angles | 105.08, 105.14, 110.28 |
Refinement procedure
Resolution | 200.000 - 2.850 |
R-factor | 0.2594 |
Rwork | 0.259 |
R-free | 0.29740 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.254 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.950 |
High resolution limit [Å] | 2.850 | 2.850 |
Rmerge | 0.050 | 0.470 |
Number of reflections | 27841 | |
<I/σ(I)> | 21 | 3.5 |
Completeness [%] | 97.3 | 96.8 |
Redundancy | 5.8 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 0.1M HEPES-NA/HCL PH 7.5 0.2M CACL2 36% PEG 400 |