5V4H
Ruthenium(II)(cymene)(chlorido)2-lysozyme adduct formed when ruthenium(II)(cymene)(bromido)2 underwent ligand exchange, resulting in one binding site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 80.320, 80.320, 36.590 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.790 - 1.220 |
| R-factor | 0.1558 |
| Rwork | 0.154 |
| R-free | 0.18990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nhi |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.430 |
| Data reduction software | iMOSFLM (7.2.1) |
| Data scaling software | Aimless (0.5.24) |
| Phasing software | PHASER (2.6.1) |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 56.790 | 56.790 | 1.240 |
| High resolution limit [Å] | 1.220 | 6.680 | 1.220 |
| Rmerge | 0.095 | 0.082 | 1.796 |
| Rmeas | 0.104 | 0.090 | 1.972 |
| Rpim | 0.039 | 0.035 | 0.783 |
| Total number of observations | 165269 | 976 | 7870 |
| Number of reflections | 32718 | 1571 | |
| <I/σ(I)> | 8.4 | 19.6 | 1 |
| Completeness [%] | 91.8 | 70.4 | 91.6 |
| Redundancy | 5.1 | 5.2 | 5 |
| CC(1/2) | 0.995 | 0.989 | 0.433 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.7 | 294 | 100mg/mL hen egg white lysozyme, 0.8 M NaCl, 0.1 M sodium acetate pH 4.7 |
