3C2X
Crystal structure of peptidoglycan recognition protein at 1.8A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 203 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-07-21 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.93 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 87.044, 101.898, 162.675 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.930 - 1.830 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yck |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.000 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.930 | 19.900 |
| High resolution limit [Å] | 1.800 | 1.830 |
| Number of reflections | 63669 | |
| Completeness [%] | 99.8 | 99.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 50mm Tris-HCl, 20% PEG3350, 0.2M Na-K Tartarate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
