3PEE
Structure of the C. difficile TcdB cysteine protease domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 128.110, 45.710, 87.350 |
| Unit cell angles | 90.00, 103.48, 90.00 |
Refinement procedure
| Resolution | 39.657 - 2.100 |
| R-factor | 0.1941 |
| Rwork | 0.192 |
| R-free | 0.24030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ho6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.308 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.220 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.073 | 0.490 |
| Number of reflections | 28295 | |
| <I/σ(I)> | 8.4 | 1.8 |
| Completeness [%] | 97.6 | 91.8 |
| Redundancy | 3.2 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1M Tris HCl pH 8.0, 30% PEG2000MME, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
