7BFC
Circular permutant of ribosomal protein S6, P54-55 truncated,
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-23 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.98013 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 85.381, 73.582, 115.796 |
| Unit cell angles | 90.00, 99.98, 90.00 |
Refinement procedure
| Resolution | 47.770 - 2.130 |
| R-factor | 0.2287 |
| Rwork | 0.227 |
| R-free | 0.26650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ris |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.901 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.21) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.900 | 47.720 | 2.200 |
| High resolution limit [Å] | 2.130 | 8.250 | 2.130 |
| Rmerge | 0.127 | 0.067 | 1.324 |
| Rmeas | 0.150 | 0.080 | 1.567 |
| Rpim | 0.080 | 0.043 | 0.830 |
| Total number of observations | 4253 | 26594 | |
| Number of reflections | 78707 | 1411 | 7695 |
| <I/σ(I)> | 8.3 | 31.1 | 1.2 |
| Completeness [%] | 99.4 | 98.3 | 99.6 |
| Redundancy | 3.4 | 3 | 3.5 |
| CC(1/2) | 0.995 | 0.993 | 0.411 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1 M HEPES pH 7.5 10% w/v PEG 8000 8% v/v ethylene glycol |
