2DJG
Re-determination of the native structure of human dipeptidyl peptidase I (cathepsin C)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-08-23 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 87.479, 88.680, 114.350 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.040 - 2.050 |
| R-factor | 0.17612 |
| Rwork | 0.174 |
| R-free | 0.22076 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k3b |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.849 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Number of reflections | 120690 | |
| Completeness [%] | 96.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 298 | 1.8M ammonium sulfate, 0.1M Na citrate, 0.2M Na/K tartrate, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
