3HFU
Crystal structure of the ligand binding domain of E. coli CynR with its specific effector azide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-02-08 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.176, 98.363, 86.272 |
Unit cell angles | 90.00, 103.77, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
Rwork | 0.223 |
R-free | 0.27430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hxr |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.613 | |
Number of reflections | 44532 | |
<I/σ(I)> | 17.78 | 3.09 |
Completeness [%] | 99.8 | 99.75 |
Redundancy | 3.7 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 294 | 25% PEG5000 monomethyl ether (MME) plus 100 mM Tris 8.5, cryoprotected in 25% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 294K |