2EC5
Crystal structures reveal a thiol-protease like catalytic triad in the C-terminal region of Pasteurella multocida toxin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-07-03 |
| Detector | MACSCIENCE |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 197.357, 132.823, 82.546 |
| Unit cell angles | 90.00, 114.74, 90.00 |
Refinement procedure
| Resolution | 44.810 - 2.600 |
| R-factor | 0.23491 |
| Rwork | 0.232 |
| R-free | 0.28632 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ebf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.208 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.094 | 0.473 |
| Number of reflections | 57847 | |
| Completeness [%] | 97.2 | 88.5 |
| Redundancy | 3.6 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 15% PEG 6000, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
