2R9F
Calpain 1 proteolytic core inactivated by ZLAK-3002, an alpha-ketoamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-24 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.569, 70.568, 110.406 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.290 - 1.600 |
| R-factor | 0.19057 |
| Rwork | 0.189 |
| R-free | 0.22174 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kxr chain A |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.273 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.460 | 1.690 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.078 | 0.602 |
| Number of reflections | 42370 | |
| <I/σ(I)> | 8.4 | 1.6 |
| Completeness [%] | 96.6 | 82.6 |
| Redundancy | 5.6 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 1.5 M NaCl, 10 mM CaCl2, and 0.1 M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
