1K0B
Ure2p in Complex with Glutathione
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-09-04 |
Detector | MARRESEARCH |
Wavelength(s) | 0.934 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.504, 124.912, 160.846 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.206 * |
Rwork | 0.207 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.250 |
Data reduction software | DENZO |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.106 * | |
Total number of observations | 353357 * | |
Number of reflections | 38915 | |
<I/σ(I)> | 6.7 | 1.6 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 4.6 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | Bousset, L., (2001) Structure, 9, 39. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | reservoir | PEG1000 | 30 (%) | |
3 | 1 | reservoir | 160 (mM) | ||
4 | 1 | reservoir | Tris | 100 (mM) |