1NU6
Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2001-11-04 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9765 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.496, 68.240, 419.289 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.100 |
R-factor | 0.21747 |
Rwork | 0.215 |
R-free | 0.26500 * |
Structure solution method | MAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.860 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 12.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.084 * | 0.268 |
Total number of observations | 234528 * | |
Number of reflections | 87113 | |
Completeness [%] | 82.9 | 72.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.5 | 293 | PEG, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG3350 | 20-25 (%) | |
3 | 1 | reservoir | 200 (mM) | ||
4 | 1 | reservoir | Tris | pH8.5 | |
5 | 1 | reservoir | glycerol | 15 (%) |