1CF9
Structure of the mutant VAL169CYS of catalase HPII from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Collection date | 1998-06-15 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 93.470, 133.040, 122.220 |
| Unit cell angles | 90.00, 109.64, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.181 * |
| Rwork | 0.181 |
| R-free | 0.23700 |
| Structure solution method | OTHER |
| Starting model (for MR) | 1iph |
| RMSD bond length | 0.001 |
| RMSD bond angle | 0.033 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.790 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.083 | 0.460 |
| Number of reflections | 250445 | |
| <I/σ(I)> | 9.6 | 2.1 |
| Completeness [%] | 88.3 | 86.7 |
| Redundancy | 3 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 9 | Bravo, J., (1995) Structure, 3, 491. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG3350 | 15 (%(w/v)) | |
| 2 | 1 | reservoir | 1.5 (M) | ||
| 3 | 1 | reservoir | Tris-HCl | 0.2 (M) |
