1E93
High resolution structure and biochemical properties of a recombinant catalase depleted in iron
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-07-15 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 108.572, 108.572, 248.760 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 * - 2.000 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1CAE |
| RMSD bond length | 0.005 |
| RMSD bond angle | 23.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.072 * | 0.220 * |
| Total number of observations | 332299 * | |
| Number of reflections | 58298 | |
| Completeness [%] | 97.8 * | 94.6 |
| Redundancy | 5.7 * | 4.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 4-5 * | drop was mixed with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 54 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 100 (mM) | |
| 3 | 1 | drop | glycerol | 5 (%(v/v)) | |
| 4 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 2 (M) | |
| 6 | 1 | reservoir | 50 (mM) |
