1CEN
CELLULASE (CELC) MUTANT WITH GLU 140 REPLACED BY GLN COMPLEXED WITH CELLOHEXAOSE
Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Detector technology | IMAGE PLATE |
Collection date | 1995-06 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.400, 84.330, 87.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.178 |
Rwork | 0.178 |
R-free | 0.24600 |
RMSD bond length | 0.009 |
RMSD bond angle | 23.300 * |
Data reduction software | DENZO |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.300 |
Rmerge | 0.089 |
Total number of observations | 105099 * |
Number of reflections | 16218 |
Completeness [%] | 94.1 |
Redundancy | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.2 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 13 (mg/ml) | |
2 | 1 | 1 | PEG2000 | 22-25 (%) | |
3 | 1 | 1 | Tris-HCl | 0.1 (M) | |
4 | 1 | 1 | cellohexaose | 10 (mM) |