1GG9
CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, HIS128ASN VARIANT.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-01-15 |
| 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 | 15.000 * - 1.890 |
| R-factor | 0.159 |
| Rwork | 0.144 |
| R-free | 0.18800 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.023 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.930 | 1.940 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.087 * | 0.275 * |
| Number of reflections | 196776 | 16215 * |
| Completeness [%] | 89.5 | 80.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 297 | PEG 3350, LiCl, Tris-HCl, pH 9.0, 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 (M) |
