4ERL
Crystal structure of the lysine riboswitch bound to a lysine-glycine dipeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2010-04-12 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 |
Unit cell lengths | 119.878, 119.878, 58.743 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.620 - 3.000 |
R-factor | 0.1974 |
Rwork | 0.195 |
R-free | 0.23380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3D0U) |
RMSD bond length | 0.007 |
RMSD bond angle | 0.933 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.620 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.113 | 0.321 |
<I/σ(I)> | 5.1 | 1.9 |
Completeness [%] | 97.8 | 96.5 |
Redundancy | 1.92 | 1.93 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 303 | 10 mM Na-HEPES pH 7.0, 2 M Li2SO4, and 5 mM MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 303K |