1ZCM
Human calpain protease core inhibited by ZLLYCH2F
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-11-15 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.440, 62.740, 99.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.182 |
| Rwork | 0.182 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kxr |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.400 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.036 | 0.103 |
| Number of reflections | 21280 | |
| <I/σ(I)> | 26.6 | 9.9 |
| Completeness [%] | 97.0 | 94.8 |
| Redundancy | 7.2 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | salting-in | 7.5 | 292 | HEPES, DTT, CaCl2, NaCl, pH 7.5, salting-in, temperature 292K |
