9YUP
Crystal structure of PprA S-F-S tetramer from Deinococcus radiodurans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-04-24 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.976250 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.679, 123.221, 139.288 |
| Unit cell angles | 90.00, 93.69, 90.00 |
Refinement procedure
| Resolution | 41.650 - 2.070 |
| R-factor | 0.2119 |
| Rwork | 0.211 |
| R-free | 0.23610 |
| Structure solution method | SAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.787 |
| Data reduction software | XDS (Jan 19, 2025 (BUILT 20250714)) |
| Data scaling software | Aimless (0.8.2) |
| Phasing software | PHASER (2.0_5824) |
| Refinement software | PHENIX (2.0_5824) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 92.207 | 2.409 |
| High resolution limit [Å] | 2.068 | 2.068 |
| Rmerge | 0.204 | 1.775 |
| Rmeas | 0.223 | 1.936 |
| Rpim | 0.067 | 0.605 |
| Number of reflections | 105944 | 5298 |
| <I/σ(I)> | 9.7 | 1.9 |
| Completeness [%] | 91.9 | 63.2 |
| Redundancy | 10.7 | 9.8 |
| CC(1/2) | 0.996 | 0.588 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293.15 | 1.0 ul of protein solution was mixed with 1.0 uL of crystallization solution and hung upside-down in a sealed chamber containing 1mL of well solution. | Protein solution: 2.4 mg/mL PprA (73 uM), 150mM KCl, 20mM Tris, pH 7.5 | Crystallization solution: 400 mM Lithium citrate, 20% (w/v) PEG 3350 | Well solution: 1.5 M Ammonium sulfate |
