1W8Q
Crystal Structure of the DD-Transpeptidase-carboxypeptidase from Actinomadura R39
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-03-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 104.560, 94.370, 106.960 |
| Unit cell angles | 90.00, 94.05, 90.00 |
Refinement procedure
| Resolution | 19.940 - 2.850 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.24400 |
| Structure solution method | OTHER |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.100 | 3.000 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.150 | 0.710 |
| Number of reflections | 47856 | |
| <I/σ(I)> | 20.7 | 2.7 |
| Completeness [%] | 98.0 | 86.7 |
| Redundancy | 13.3 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
