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 |






