2B4L
Crystal structure of the binding protein OpuAC in complex with glycine betaine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Wavelength(s) | 1.05 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 29.818, 88.486, 95.714 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 17.000 - 2.000 |
Rwork | 0.201 |
R-free | 0.25520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Selenomethionine derivative |
RMSD bond length | 0.009 |
RMSD bond angle | 1.129 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0000) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 17.000 | 2.020 |
High resolution limit [Å] | 1.980 | 1.980 |
Rmerge | 0.111 | |
Number of reflections | 18948 | |
<I/σ(I)> | 6 | |
Completeness [%] | 98.9 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.25 | 274 | Tris, ammonium acetate, PEG 4000, pH 8.25, VAPOR DIFFUSION, HANGING DROP, temperature 274K |