2EBH
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 | 2006-05-22 |
Detector | MACSCIENCE |
Wavelength(s) | 0.9 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 110.755, 150.559, 77.910 |
Unit cell angles | 90.00, 104.54, 90.00 |
Refinement procedure
Resolution | 43.690 - 2.400 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.24940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ebf |
RMSD bond length | 0.007 |
RMSD bond angle | 1.069 |
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 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.094 | 0.403 |
Number of reflections | 47787 | |
Completeness [%] | 99.1 | 93.5 |
Redundancy | 3.8 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 1.0M ammonium citrate, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |