4OX3
Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-09-28 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.969 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.644, 53.695, 102.330 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.170 - 2.000 |
| R-factor | 0.20715 |
| Rwork | 0.205 |
| R-free | 0.25137 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.869 |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 51.170 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Number of reflections | 25369 | |
| <I/σ(I)> | 11.9 | |
| Completeness [%] | 95.7 | 89.3 |
| Redundancy | 3.2 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | 295 | 0.1 M phosphate/citrate buffer, pH 4.2, 40 % PEG 300 |
