5IHG
The X-ray structure of the adduct formed in the reaction between hen egg white lysozyme a compound I, a platin(II) compound containing a O, S bidentate ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR571 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-12-01 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 77.575, 77.575, 37.253 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 54.850 - 1.750 |
| R-factor | 0.164 |
| Rwork | 0.162 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4j1a |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.817 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.850 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.058 | 0.507 |
| Number of reflections | 11472 | |
| <I/σ(I)> | 44.1 | 2.3 |
| Completeness [%] | 95.3 | |
| Redundancy | 6.2 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.4 | 298 | 1.1 M NaCl, 0.1 M sodium acetate pH 4.4. S protein concentration :about 15 mg/ml. |
