4A1J
Ykud L,D-transpeptidase from B.subtilis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-22 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 56.240, 86.280, 74.140 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.115 - 2.200 |
| R-factor | 0.1974 |
| Rwork | 0.192 |
| R-free | 0.24370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1y7m |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.072 |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.400 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.100 | 0.370 |
| Number of reflections | 18649 | |
| <I/σ(I)> | 16.1 | 6.5 |
| Completeness [%] | 98.4 | 88.7 |
| Redundancy | 11.7 | 11.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 100 MM BIS-TRIS PH 5.5, 200 MM AMSO4, 25 % PEG 3350 AND 2 MM MURNAC MONOSACCHARIDE. |






