7S02
Crystal structure of FBF-2 in complex with LST-1 site A peptide and FBE RNA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-07-12 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 61 |
Unit cell lengths | 93.813, 93.813, 113.222 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.120 - 2.340 |
R-factor | 0.1823 |
Rwork | 0.178 |
R-free | 0.22470 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3k5q |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.380 |
High resolution limit [Å] | 2.340 | 6.350 | 2.340 |
Rmerge | 0.080 | 0.049 | 0.767 |
Rmeas | 0.090 | 0.055 | 0.853 |
Rpim | 0.039 | 0.024 | 0.370 |
Total number of observations | 120279 | ||
Number of reflections | 23853 | 1230 | 1191 |
<I/σ(I)> | 9.7 | ||
Completeness [%] | 99.7 | 99.8 | 99.9 |
Redundancy | 5 | 5.3 | 5.2 |
CC(1/2) | 0.994 | 0.711 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 25% (v/v) PEG 400, 0.1 M Tris, pH 8.5 |