1CLX
CATALYTIC CORE OF XYLANASE A
Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 291 |
Detector technology | IMAGE PLATE |
Collection date | 1993-01-11 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 96.110, 97.320, 151.030 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.800 |
R-factor | 0.166 * |
Rwork | 0.166 |
RMSD bond length | 0.008 * |
RMSD bond angle | 0.027 * |
Data reduction software | DENZO |
Refinement software | RESTRAIN |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 6.920 * | |
High resolution limit [Å] | 1.790 * | 1.790 * |
Rmerge | 0.077 | 0.479 * |
Total number of observations | 703625 * | |
Number of reflections | 105167 | 7963 * |
Completeness [%] | 78.8 | 61.5 * |
Redundancy | 6.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | pH 7.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 23.3 (mg/ml) | |
2 | 1 | drop | PEG3400 | 2.2-2.7 (%) | |
3 | 1 | drop | phosphate | 66.7 (mM) | |
4 | 1 | reservoir | PEG3400 | 10-12 (%) | |
5 | 1 | reservoir | phosphate | 200 (mM) |