2NSM
Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.05 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 150.030, 150.030, 54.910 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.100 |
| R-factor | 0.1789 |
| Rwork | 0.179 |
| R-free | 0.20080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h8l |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.270 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.170 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.068 | 0.280 |
| Number of reflections | 41723 | |
| <I/σ(I)> | 15.26 | 4.37 |
| Completeness [%] | 99.4 | 99.4 |
| Redundancy | 3.36 | 3.35 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 0.1M Hepes, 2M Ammonium sulfate, 5mM EDTA, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
