4I05
Structure of intermediate processing form of cathepsin B1 from Schistosoma mansoni
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-10 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 93.859, 50.988, 62.546 |
| Unit cell angles | 90.00, 91.31, 90.00 |
Refinement procedure
| Resolution | 25.520 - 1.900 |
| R-factor | 0.16587 |
| Rwork | 0.163 |
| R-free | 0.21642 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qsd |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.487 |
| 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 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.082 | 0.350 |
| Number of reflections | 23559 | |
| <I/σ(I)> | 18.2 | |
| Completeness [%] | 99.4 | 98.7 |
| Redundancy | 3 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | Reservoir: 0.2M Ammonium Acetate, 0.1M Sodium Citrate, 30% PEG 4000. Protein buffer and concentration: 5mM Sodium Acetate, pH 5.5, Cpr=1.5mg/ml. Ratio Protein: Reservoir=1:0.75. Cryocooled in mother liquor., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
