1W79
Crystal structure of the DD-transpeptidase-carboxypeptidase from Actinomadura R39
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-03-01 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 105.187, 93.369, 107.272 |
| Unit cell angles | 90.00, 94.25, 90.00 |
Refinement procedure
| Resolution | 19.950 - 1.800 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| R-free | 0.24000 |
| Structure solution method | OTHER |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.700 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.100 | 0.500 |
| Number of reflections | 187527 | |
| <I/σ(I)> | 4.2 | 1.8 |
| Completeness [%] | 98.5 | 95.6 |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 |
