1US3
Native xylanase10C from Cellvibrio japonicus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-11-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 44.175, 78.789, 172.244 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.850 |
R-factor | 0.162 |
Rwork | 0.160 |
R-free | 0.20000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1clx |
RMSD bond length | 0.016 |
RMSD bond angle | 1.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.088 | 0.310 |
Number of reflections | 52228 | |
<I/σ(I)> | 16.4 | 5.6 |
Completeness [%] | 99.0 | 98 |
Redundancy | 5.0 * | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 18 * | 30 MG/ML PROTEIN 0.2 M SODIUM IODIDE, 20% PEG 3350, pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | reservoir | sodium iodide | 0.2 (M) | |
3 | 1 | reservoir | PEG3350 | 20 (%(w/v)) |