1TK3
Crystal Structure Of Human Apo Dipeptidyl Peptidase IV/CD26
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 119.264, 122.360, 129.823 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.680 - 2.000 |
| R-factor | 0.229 |
| Rwork | 0.229 |
| R-free | 0.27200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n1m |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNX (2000.1) |
| Refinement software | CNX (2000.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.680 | 2.130 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 116526 | |
| Completeness [%] | 90.6 | 79.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | PEG 4000, SODIUM ACETATE, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






