2XZ4
Crystal structure of the LFZ ectodomain of the peptidoglycan recognition protein LF
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-11-30 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 74.802, 113.443, 37.532 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.747 - 1.720 |
| R-factor | 0.1655 |
| Rwork | 0.164 |
| R-free | 0.20140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2F2L CHAIN X |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.084 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.170 | 1.810 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.050 | 0.360 |
| Number of reflections | 34205 | |
| <I/σ(I)> | 15.3 | 2.9 |
| Completeness [%] | 98.6 | 96.5 |
| Redundancy | 3.5 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 30% PEG300, 0.1M SODIUM CACODYLATE PH6.0 |
