2ISA
Crystal Structure of Vibrio salmonicida catalase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-07-07 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.874 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 98.150, 217.760, 99.280 |
| Unit cell angles | 90.00, 110.48, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.970 |
| R-factor | 0.15082 |
| Rwork | 0.148 |
| R-free | 0.20034 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m85 mutated to fit the Vibrio salmonicida catalase sequence |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.268 |
| Data reduction software | XDS |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.089 | 2.060 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Rmerge | 0.111 | 0.361 |
| Number of reflections | 267579 | |
| <I/σ(I)> | 6 | 2 |
| Redundancy | 2.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 2.0M Ammonium sulphate, 2% PEG400, 100mM Na-Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
