5OBG
Crystal structure of glycine binding protein in complex with strychnine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 150 |
Detector technology | CCD |
Collection date | 2017-04-11 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54157 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 90.353, 100.040, 163.752 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.920 - 2.000 |
R-factor | 0.19928 |
Rwork | 0.197 |
R-free | 0.24961 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5oan |
RMSD bond length | 0.018 |
RMSD bond angle | 1.950 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.920 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.147 | 0.589 |
Number of reflections | 100843 | 4919 |
<I/σ(I)> | 6.1 | 1.9 |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.2 | 6.2 |
CC(1/2) | 0.992 | 0.657 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Reservoir buffer: 20 % PEG 3350, 0.2 M MgOAc Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 0.5 mM strychnine |