2EBF
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 | 2005-10-06 |
| Detector | MACSCIENCE |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 110.971, 150.406, 77.139 |
| Unit cell angles | 90.00, 105.46, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.23278 |
| Structure solution method | SIRAS |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.189 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.097 | 0.448 |
| Number of reflections | 93581 | |
| Completeness [%] | 97.3 | 81.3 |
| Redundancy | 3.6 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 1.6M ammonium phosphate, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
