1PFQ
crystal structure of human apo dipeptidyl peptidase IV / CD26
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.031, 118.142, 184.583 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.25614 |
| Rwork | 0.254 |
| R-free | 0.29800 * |
| Structure solution method | MIR |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.650 * |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | |
| High resolution limit [Å] | 1.900 | |
| Rmerge | 0.126 * | 0.648 * |
| Total number of observations | 803624 * | |
| Number of reflections | 122631 | |
| Completeness [%] | 99.7 | 100 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG3350 | 25 (%) | |
| 2 | 1 | reservoir | 200 (mM) | ||
| 3 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
| 4 | 1 | drop | Tris | 25 (mM) | pH7.5 |
| 5 | 1 | drop | 100 (mM) | ||
| 6 | 1 | drop | TCEP | 2 (mM) | |
| 7 | 1 | drop | glycerol | 5 (%) | |
| 8 | 1 | drop | protein | 20 (mg/ml) |






