4ZPU
The structure of DLP12 endolysin exhibits likely active and inactive conformations.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2015-03-20 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 78.106, 94.131, 97.430 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.400 |
| R-factor | 0.22393 |
| Rwork | 0.221 |
| R-free | 0.28459 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hde |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.632 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.111 | 0.830 |
| Number of reflections | 28659 | |
| <I/σ(I)> | 2.2 | 2.2 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 11.2 | 9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293.15 | 0.1M Sodium acetate pH 4.8, 2.1M Sodium formate, Protein concentration-25mg/ml. |
