4I04
Structure of zymogen of cathepsin B1 from Schistosoma mansoni
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.914 |
| Spacegroup name | P 1 |
| Unit cell lengths | 54.281, 83.172, 84.569 |
| Unit cell angles | 76.97, 86.60, 71.11 |
Refinement procedure
| Resolution | 38.400 - 1.950 |
| R-factor | 0.20195 |
| Rwork | 0.199 |
| R-free | 0.25245 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qsd |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.303 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.037 | 0.296 |
| Number of reflections | 78650 | |
| <I/σ(I)> | 25.9 | 3.1 |
| Completeness [%] | 78.4 | 42.1 |
| Redundancy | 2.3 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | Reservoir: 0.1M Ammonium Acetate, 0.1M Bis-Tris, 17% PEG 10000. Protein buffer and concentration: 5mM Sodium Acetate, pH 5.5, Cpr=5.25mg/ml. Ratio Protein: Reservoir=2:1. Cryocooled in mother liquor containing 20% ethylene glycol., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
