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 |