1WM3
Crystal structure of human SUMO-2 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL17B2 |
Synchrotron site | NSRRC |
Beamline | BL17B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-07-07 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.0717 |
Spacegroup name | H 3 |
Unit cell lengths | 74.964, 74.964, 33.231 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.200 |
R-factor | 0.122 |
Rwork | 0.119 |
R-free | 0.18500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wm2 |
RMSD bond length | 0.013 |
RMSD bond angle | 2.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.046 | 0.559 |
Number of reflections | 21781 | |
<I/σ(I)> | 39.6 | 2.6 |
Completeness [%] | 100.0 | 99.8 |
Redundancy | 6.49 | 5.24 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 40% PEG600, 0.1M CHES, 0.1M Na-HEPES, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |