1KS5
Structure of Aspergillus niger endoglucanase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1994-10-01 |
Detector | MAC Science DIP-2030K |
Wavelength(s) | 1.5418 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 131.570, 131.570, 71.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 * - 2.100 |
Rwork | 0.175 |
R-free | 0.19600 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 * |
RMSD bond angle | 1.340 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 * | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.070 | 0.300 |
Total number of observations | 325097 * | |
Number of reflections | 18660 * | |
Completeness [%] | 98.0 * | 95.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 291 | PEG 4000, Sodium Acetate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 9 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 28 (%) | |
3 | 1 | reservoir | acetate | 100 (mM) | pH4.8 |