6F37
Fusion protein of RSL and trimeric coiled coil
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 2 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-02-11 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.980 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 88.760, 88.760, 88.760 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.810 - 2.200 |
| R-factor | 0.2096 |
| Rwork | 0.208 |
| R-free | 0.24690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2BT9 chain A |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.013 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.27) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 88.760 | 88.760 | 2.270 |
| High resolution limit [Å] | 2.200 | 9.070 | 2.200 |
| Rmerge | 0.178 | 0.065 | 0.511 |
| Rmeas | 0.185 | 0.069 | 0.531 |
| Rpim | 0.051 | 0.023 | 0.141 |
| Number of reflections | 12123 | 204 | 1019 |
| <I/σ(I)> | 21.6 | ||
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 13.2 | 9 | 14 |
| CC(1/2) | 0.997 | 0.998 | 0.554 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293.15 | 20% PEG 8000, 0.1 M CHES pH 9.5 |






