1GGF
CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, VARIANT HIS128ASN, COMPLEX WITH HYDROGEN PEROXIDE.
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 | 93.372, 133.415, 121.918 |
Unit cell angles | 90.00, 109.63, 90.00 |
Refinement procedure
Resolution | 19.800 * - 2.280 |
R-factor | 0.185 |
Rwork | 0.174 |
R-free | 0.25400 |
RMSD bond length | 0.009 |
RMSD bond angle | 0.031 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.840 | 2.340 |
High resolution limit [Å] | 2.280 | 2.280 |
Rmerge | 0.107 * | 0.365 * |
Number of reflections | 125885 | 9488 * |
Completeness [%] | 98.5 | 95.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 9 | 297 | PEG 3350, LiCl, Tris-HCl. Before data collection the protein crystal was soaked during a few seconds in the solution with 2M hydrogen peroxide., pH 9.0, 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) |