1GGE
CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, NATIVE STRUCTURE AT 1.9 A RESOLUTION.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-01-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 93.040, 132.340, 121.200 |
| Unit cell angles | 90.00, 109.63, 90.00 |
Refinement procedure
| Resolution | 18.000 * - 1.890 |
| R-factor | 0.166 * |
| Rwork | 0.163 |
| R-free | 0.20200 |
| RMSD bond length | 0.008 * |
| RMSD bond angle | 0.025 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.960 | 1.940 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.089 * | 0.269 * |
| Number of reflections | 214389 | 16094 * |
| Completeness [%] | 97.7 | 88.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 297 | PEG 3350, LiCl, Tris-HCl, pH 9.00, VAPOR DIFFUSION, HANGING DROP, temperature 297.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | reservoir | PEG3350 | 15-17 (%) | |
| 3 | 1 | reservoir | 1.6-1.5 (M) | ||
| 4 | 1 | reservoir | Tris-HCl | 0.1 (0.1) |






