5DDO
Structural and Dynamic Basis for Low Affinity-High Selectivity Binding of L-glutamine by the Gln-riboswitch
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-01-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9792 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 80.840, 99.652, 88.461 |
Unit cell angles | 90.00, 99.05, 90.00 |
Refinement procedure
Resolution | 39.917 - 3.100 |
R-factor | 0.2305 |
Rwork | 0.227 |
R-free | 0.28870 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | U1A protein |
RMSD bond length | 0.008 |
RMSD bond angle | 1.261 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.210 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.088 | 0.479 |
Number of reflections | 12813 | |
<I/σ(I)> | 15.7 | 2.5 |
Completeness [%] | 99.7 | 99.5 |
Redundancy | 4.1 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 293 | 0.2 M Na-formate, 21% (w/v) PEG3350 |