9QIY
Crystal structure of the S-adenosyl-L-homocysteine hydrolase from P. aeruginosa, Q65N mutant probed with rubidium to confirm disruption of a potassium binding site.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-12-11 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.81301 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 176.592, 104.666, 107.809 |
| Unit cell angles | 90.00, 100.34, 90.00 |
Refinement procedure
| Resolution | 37.250 - 1.910 |
| R-factor | 0.1753 |
| Rwork | 0.175 |
| R-free | 0.21460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.926 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | REFMAC |
| Refinement software | PHENIX (1.21.2_5419+SVN) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.400 | 2.030 |
| High resolution limit [Å] | 1.910 | 1.910 |
| Rmerge | 0.112 | 1.030 |
| Rmeas | 0.132 | 122.900 |
| Number of reflections | 288982 | 44199 |
| <I/σ(I)> | 8.59 | |
| Completeness [%] | 98.0 | 92.6 |
| Redundancy | 3.46 | |
| CC(1/2) | 0.996 | 0.520 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 50 mM KH2PO4, 20% (w/v) PEG8000, 20% (v/v) glycerol |
