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 |