2R9C
Calpain 1 proteolytic core inactivated by ZLAK-3001, 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 | 40.430, 70.250, 110.410 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.600 - 1.800 |
| R-factor | 0.15818 |
| Rwork | 0.156 |
| R-free | 0.19570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kxr chain a |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.467 |
| 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] | 59.235 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.040 | 0.122 |
| Number of reflections | 29944 | |
| <I/σ(I)> | 14.9 | 15.1 |
| Completeness [%] | 99.2 | 99.4 |
| Redundancy | 6.6 | 6.7 |
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 |
