9CFS
Structure of a 150% lengthened variant of the E. coli ROP protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X17B1 |
| Synchrotron site | NSLS |
| Beamline | X17B1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-10-04 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 32 |
| Unit cell lengths | 43.253, 43.253, 84.158 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 22.450 - 1.750 |
| R-factor | 0.20211 |
| Rwork | 0.199 |
| R-free | 0.25602 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.049 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.450 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.121 | 0.407 |
| Rmeas | 0.129 | 0.458 |
| Rpim | 0.044 | 0.205 |
| Total number of observations | 138359 | 4404 |
| Number of reflections | 17737 | 942 |
| <I/σ(I)> | 10.9 | 2.8 |
| Completeness [%] | 99.7 | |
| Redundancy | 7.8 | 4.7 |
| CC(1/2) | 0.996 | 0.817 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.2 | 290 | 200 mM Na Phosphate 30% PEG 300 |
