5FIR
Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 170.210, 200.770, 202.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.393 - 2.836 |
R-factor | 0.1867 |
Rwork | 0.185 |
R-free | 0.23760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HOMOLOGY MODEL |
RMSD bond length | 0.011 |
RMSD bond angle | 1.180 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.910 |
High resolution limit [Å] | 2.840 | 2.840 |
Rmerge | 0.130 | 1.260 |
Number of reflections | 155519 | |
<I/σ(I)> | 7.1 | 0.75 |
Completeness [%] | 94.6 | 84.5 |
Redundancy | 3.2 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 2M AMMONIUM SULFATE, 0.1 M BIS-TRIS PH 6.5 |