3KJF
Caspase 3 Bound to a covalent inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 96.690, 68.160, 44.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.710 - 2.000 |
| R-factor | 0.18322 |
| Rwork | 0.181 |
| R-free | 0.20649 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.347 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 16700 | |
| Completeness [%] | 89.2 | 60.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.8 | 277 | Inhibitor (2 microliters of a 100 mM DMSO stock) added to 100 microliters of protein (6.5 mg/mL) in 20 mM Tris, 10 mM DTT pH 8.0. Drops contained equal volumes of protein and well solution (16% ethanol, 0.1 M Tris pH 7.8), VAPOR DIFFUSION, temperature 277K |
