3FVY
Crystal structure of human Dipeptidyl Peptidase III
Experimental procedure
| Experimental method | SAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.28267 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.812, 151.378, 53.721 |
| Unit cell angles | 90.00, 100.04, 90.00 |
Refinement procedure
| Resolution | 75.590 - 1.900 |
| R-factor | 0.17234 |
| Rwork | 0.172 |
| R-free | 0.21939 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3csk |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.218 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.107 | 0.780 |
| Number of reflections | 61597 | |
| <I/σ(I)> | 7.1 | 1.93 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 297 | 20% PEG3350. 0.2M MgForm, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
