3DLJ
Crystal structure of human carnosine dipeptidase 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.96749 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.106, 75.613, 103.716 |
| Unit cell angles | 90.00, 109.79, 90.00 |
Refinement procedure
| Resolution | 29.910 - 2.260 |
| R-factor | 0.20109 |
| Rwork | 0.200 |
| R-free | 0.25402 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zof |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.364 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.061 | 0.401 |
| Number of reflections | 51418 | |
| <I/σ(I)> | 11.6 | 2.3 |
| Completeness [%] | 97.4 | 85.4 |
| Redundancy | 3.6 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 297 | 30% PEG 4000, 0.2M Ammonium sulfate, 0.1M Na Cacodylate pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
