1R9N
Crystal Structure of human dipeptidyl peptidase IV in complex with a decapeptide (tNPY) at 2.3 Ang. Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 173 |
| Detector technology | CCD |
| Collection date | 2003-03-15 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.01 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 122.606, 122.701, 145.405 |
| Unit cell angles | 90.00, 114.88, 90.00 |
Refinement procedure
| Resolution | 41.170 - 2.300 |
| R-factor | 0.2127 |
| Rwork | 0.211 |
| R-free | 0.25140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | : 1R9M |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.276 |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23270.000 | 2.360 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.075 | 0.429 |
| Number of reflections | 161260 | |
| <I/σ(I)> | 11.7 | 1.8 |
| Completeness [%] | 94.2 | |
| Redundancy | 2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.25 | 298 | PEG 2000, Bicine, pH 8.25, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
