2I7A
Domain IV of Human Calpain 13
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-08-18 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 86.115, 86.115, 47.417 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.000 - 1.800 |
R-factor | 0.17054 |
Rwork | 0.169 |
R-free | 0.19699 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kfu |
RMSD bond length | 0.017 |
RMSD bond angle | 1.496 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 18860 | |
<I/σ(I)> | 33.18 | 1.2 |
Completeness [%] | 99.0 | 89.6 |
Redundancy | 9.6 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 25% PEG4K, 0.2M NH4SO4, 0.1M Na-Ac, 10 mg/mL protein solution, cryoprotected with 25% glycerol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |