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 |